Isoelectric points and molecular weights of proteins

ESOEEECTRIC

POfNTS

AND

MOLECULAR

WEKZWS

OF PROTEINS

A TABLE

PIER GIORGKO RiGHETFI and TIZZANA CAECAVAGGIO Departmpnrof Efachemis~~y,Univprsi~yof Milan, Via Celoria _5 Milan 20133 (%=&_I (Received December 2nd, 1975)

CONTENTS 1.Intmduction_......... ._.__ _.___ A. MeasurementofpK in iwekctric fccusing _ . . . B. pH measuremenbafter IEF in density gradients _ . C. pNmeasurementsafterIEFinge!media _ _ _ _ _ D.UseofpHmzrkers _. _ _ _ _ _ . . . _. . 2.AcknowIedgement.._..... ___._._..._ 3.SUrn~.................................... References _ . _ _ _ _ _ _ _ _ _ _ _ _ _ . _ . . .

.___.

. _ . . _ _ _.

. _ _ .

_ . _ .

_ _.......

. _ . .

. _ . .

_ _ . _

_.......__

_ . _ . _ . _.

. _ . .

. . _ .

I

_ _ .

_ . . _

. . _ _ . _.

. _ _ -

_.

_ _ _ _ _ _ _ _ _ _ . _ . . _ .

2 3 4

5 22 22 22

1. INTRODUCTION

The aim of this article is to provide a list of proteins having known macromolecular parameters, with particular emphasis on isoelectric points (pl) and molecular weights (M-W.). The new updated revision of the classical tabfes of D~FI~ and Klotz’ now has more than 500 entries, each complete with the native molecular weight of the macromolecule, as well as its subunit number and M.W. For each entry, these workers also list the source and, when applicable, the organ of origin. This is very important, since lack of this information in previous tables has generated confusion. The main aim of DarnaH and Klot$ was to tabulate proteins having a known quaternary structure. Similar tables have been published by Klein$. However, there is no literature compilation of information on the charge (pl) as well as on the size (M.W.) of proteins. Yet, the pl of a protein is a very important parameter, and its knowledge is very important for the proper use of several techniques, such as disc electrophoresis, isotachophoresis, isoelectric focusing, ion-excharzgechromatography and even ammonium sulphate fractionation. Until recently, the literature data on pf values of proteins were scanty and even contradictory. With the advent of isoelectric focusing34, pf data for proteins have been rapidly expanding, to an extent which justifies their collection in- a tabie. Thus, the main emphasis here is on the availability and collection of proteiir pl values. When available, we also report their M.W. values and quaternary structure. The coribined knowiedge of these two parameters makes possible the macromoIecuIar zapping of proteins’. Most proteins, in fact, are urtequivoeally determined by values of their pf and M.W. (except, perhaps,

P. G. RIGHETTI,

2

T. CARAVAGGIQ

for very close genetic variants of a protein, such as human haemoglobin).

Many of the entries in our tables, which lack data on M.W. and subunit structure, can be found in the tables of Damall and Klotzl. However, for the same protein the source and/or the organ may be difierent; therefore we decided not to report such data. Since most of the proteins reported display microheterogeneity, we have marked the main components with an asterisk when this information was available or could be deduced from graphs or tables. In addition, we also report not only the source and the organ, but also the intracellular Iocation, in the case of isozymes displaying different properties in different subcellular compartments. Unfortunately, there is quite a degree of uncertainty as to the temperature of pH measurement. This is quite an important parameter when defining the p1 of a protein, since acid-base equilibria are temperature dependent and a pL of a protein, if quoted without the temperature of measurement, is per se ambiguous and lacks an exact physicochemical signticance. Some workers never report the temperature of pH measurement. Most workers simply refer to measurements performed at room temperature, which, unfortunately, is not unequivocally determined_ Only a few workers have made pH measurements at a precise temperature, in a thermostatted vessel. Since the way in which a pH measurement is made is of utmost importance in def%riug PI, we summarize here the different techniques used, either in liquid or in gel media. (A) Meamremem

of pH in isoelectric focusing

The pI of a protein determined by isoelectric focusing (IEF) also represents its isoionic point in the absence of complex-forming ionss. By detiition, the isoionic point is a measure of the intrinsic acidity of a pure protein, as it is de&red as that pH which does not change on addition of a small amount of pure protein9. This definition is also applicable to a protein analyzed by LEF, as the pH of the isoelectric zone does not alter on addition of more protein. it should be remembered that pI values estimated by IEF are temperature dependent and usually decrease with increasing temperature6. The difference in pI for the same protein, measured at 25 and at 4”, could be as high as 0.5 pH units, the higher value being obtained at the lower temperature. This difference is usually more pronounced in alkaline regions, and when a protein has a pI value close to the pK of some of its functional groups. Unfortunately, when given a pE value for a protein at a certain temperature it is difficult to extrapolate this value to another temperature, since the temperature coefficient, dpI/d7’, can vary from protein to protein. Thus Bours’*, by measuring the pI values of @-lactoglobulin A and B at 4 and 25”, found a value of dpI/dT of -(0.9 + 0.2). IO-” pH unit per degree. On the other hand, measurements of pl at 4 and 25” for carbonic anhydrase have given a dpI/dT value of -(l-3 f 0.2). lo-’ pH unit per degree. In the case of myogiobin I*, the temperature coefficient is as high as - 1.7 - lo-’ pH unit per degree. Ideally, pH measurements should be made at the same temperature used during the IEF separation, since in IEF the temperature coefficient, dpT/dT, refers to the corresponding carrier ampholytes rather than to the protein contained in a given fraction. In fact, at the usual concentration of Ampholine (I%), the buffering capacity of the carrier ampholytes in the isoelectric state will normally be su&ient to permit them to dictate the pH even in the presence of as much as 1 oA of proteir&=. This

ISOELECTRIC

POW-i-S AND

MOLECULAR

WEIGHTS

OF PROTEINS

3

means that the pH vatue assigned to the concentration maximum of 2 focused protein at a temperature different from the IEF temperature will refer to the corresponding different protolytic ampholyte fraction rather than to the protein ls_ Furthermore, groups are known to display widely different degrees of temperature dependence in their dissociation constants (as a consequence of Iarge differences in their standard heats of ionization)l’. Thus, once a protein has been focused at 4”, a pd measurement made at 20 or at 25” may not represent the true pI of the protein or the pE of the Ampholine molecules surrounding it. In addition, pH measurements can also be affected by the presence of solutes such as glycerol and sucrose, which are common!y used in IEF. As sucrose lowers the dieiectric constant of the solvent and this, in turn, causes the pK values of amino acids to increase15, it can be expected that the p! value of a given protein is increased on increasmg the concentration of sucrose. When TEF is performed in the presence of urea, it should be noted that urea appreciably decreases the activity coefficient of hydrogen ions, resulting in apparently higher pK and pl values of the carrier amphofytes. Correction factors should therefore be used for pl determinations of proteins in ureax6_ (B) pH meczswements

afrer IEF in density

grdients

En preparative IEF in liquid support media, combined UV and pH readings of a!! of the collected fractions can be a lengthy and cumbersome procedure. To overcome this, Jonsson et cr1.l’ automated the analysis of column contents by pumping them at a constant rate through series-coupled flow cells, one cell for the recording of pH and the other cell for the determination of UV absorbance. This set-up, however, presented some difficulties in pH determination, which are discussed in detail by these workers l’. LMore recently, Secchi Is described a modification of this technique, which appears to overcome many of the problems. A combined glass electrode (ingold Type 401-M7, provided with a Sow vessel and water cooling jacket) is coupled ir, series with the UV Sow cell of an LKB Uvicord If. In this case, the UV signal and pH readings are fed, via a control unit, to the same galvanometric recorder used for the UV readings (LKB 6500). Since the volume lag between the pH and UV cells is only 0.35 m!, accurate and simultaneous pH and UV readings are obtained on the same recorder chart. Moreover, since the pH cell is thermostatted, pH readings are made at the temperature of the focusing column. Another advantage of flow systems is that absorption of carbon dioxide from the air, which might aKer.t pI readings by lowering the pH of the solution, especially in alkaline regions, is 2~ oided. A simiiar set-up was reported by Strongin et al.19, who brdt a pH flow cell in Ferspex with Type K-401 and Type GK 2320~ pH electrodes. from Radiometer A/S. When using Aow cells, the peristaltic pump should be attached after the cells, in order to prevent leakage of potassium chloride from the e!ectrlJdes and to keep the Sow-rate as low as possible (to avoid pressure on the glass membl ane of the electrode, which could alter the pH readings). Alternatively, for measurem-nt of the pH course in a micro-column, where fractions of only 60 ~1 are colkcted, FredrikssorGO described the use of a Radiometer micro glass electrode, in which the pH-sensitive membrane is shsped as a horizontal capillary. The capillary can be filled, via a vertical poiyethylene tube, simp!y by suction. A volume as sma!! as 20 p! is sufficient for pH reading. Values correct to within O-O! pH unit have been reported.

4

P. G. RIGKETE1, T. CARAVAGGEO

When performing IEF in solid support media, it is convenient to be able to measure directly the pH gradient along the gel length. For flat gels, a surface electrode may be used with a coplanar glass reference electrode- haviug either a flat face or a spear tip. In either case, it is advisable to have the probes of both electrodes as close as possible to minimize errors due to differences in conductivity throughout the gel. One of the first electrodes developed for pM measurements on gel surfaces is the antimony micro-electrode, in conjunction with a calomel reference electrode, reported by Beeley et al. 2L. This electrode, which was originally developed by Kleinberg= to measure the pH of dental plaques, has a spear tip of 1 mm in diameter. Measlltements are made by placing the gel over a sheet of graph paper, pressing the reference electrode at any position along the gel length and scanning at regular intervals with the antimony micro-electrode. Where the pII reading has been made, the gel is marked by serration with a scalpel blade. This allows a much greater accuracy in the determination of pI by interpolation on a graph of PI-I ve~stlsprotein position in the gel. With the antimony electrode, readings of electromotive force are obtained on the millivolt scale and are converted into units of pH by means of an appropriate calibration graph. This type of electrode might be better standardized against Ampholine solutions, which in turn are calibrated against standard bufferP_ One important property of the antimony micro-electrode, in contrast to very small glass electrodes, is its rapid equilibration time (less than 10 set), even at low temperatures, which makes it very attractive for use at 4”. However, one disadvantage of this electrode is its low reproducibility, given by Beeley et al,” as < O-25 pH units, in comparison with the resolution of 0.02 pH units, and even less, afforded by IEF. Alternatively, on gel slabs, the pH can be measured directly on the gel surface with a flat membrane electrode, such as LOT Type 403-3U-MS frcm Ingold. However, since this electrode has a high sul-face area (membrane diameter, S mm), DrysdaIe** (in collaboration with Ingold Inc., Lexington, Mass., U.S.A.) has developed a flat membrane micro-electrode. This h-shaped electrode contains the reference unit in one arm, and the measuring membrane in a parallel arm. The two electrodes are coplanar, and are on@ 3 mm apart in order to offset variations in conductivity along the gel. The pH membrane has a diameter of 2.5 mm. This allows accurate pH measurements over a small surface; however, due to the high impedance of the small glass membrane, this electrode is practically of no use at low temperatures, since the response times are extremely long. -In order to overcome the problems connected with the use of surface electrodes, we have devised a simple method for accurate pH measurements in gel slabs, using a standard combination micro-electrode. The gel slab is focused over plastic graph paper placed on the coolm g block of an LKB Multiphor 2117 apparatus, thermostatted at 4”. At the end of the experiment, 22 OF 23 gel segments are cut from the side of the gel, at 0.5-cm intervals. Simultaneously, a l-2-mm diameter hole is bored in the gel (with the help of a gel puncher for immunodi&tsion and of a suction pump) in a zone corresponding to the middle of the 05cm gel segment removed for pH measurement. Since this operation is made on the cooling block, and requires only a few minutes, no appreciable diffusions of the protein zones takes place. The rectangular gel segments removed are eluted in small test-tubes with 0.3 ml of i0 mv

ISOELECTRIC POINTS AND MOLEC~AR

WEIGHTS OF PROTEINS

5

KCZ. Since the combination micro-electrode, with a saturated solution of KC1 and buffers, is kept in the cold room (connected to the electronic control unit outside by a cabfe passing through the wall), accurate and reproducible pH measurements are obtained from the gel eluates at the focusing temperature. The pH profile can be easily superimposed on the stained gel slab with the aid of the 22 or 23 holes punched in it. [D)

Use

of pH

markers

An alternative to pH measurements along the gel length, especially when working with thin-layer equipment, is the use of a calibrated mixture of pH markers, TABLE 1 pH MARRERS FOR lSOELECTRIC FOCUSING

Proteins

cyto&rome

c

Ribonuclease Myoglobin (sperm whale) : major component minor component Myoglobin (horse) : major component minor component Bovine haemoglobin A Carbonic anhydrase (bovine) Conalbumin &Lzctoglobuhn B &Lactoglobulin A Bovine insulin Albumin (bovine) Cohn: fraction 5 Ovalbumin Horse spleen ferritin I Morse spleen ferritin 11 Horse spleen ferritin III Dyes

9.28 f 0.02’ 8.88 +=0.03’ 8.i8 + 0.02’; 8.18 & 0.04*7.68 i 0.02’ 7.33 I 0.01’; 7.45 & o.@%-* 6.88 f 0.02’; 7.15 + o.W* 6.80”’ 5.88 c 0.02’ 5.31’ 5.14 & 0.01’ 5.32 i 0.02”’ 4.90”’ 4.70”’ 4.50 & 0.02’ 4.38 i 0.02’ 4.23 & 0.03’

Iris(S-hydroxy-l.fO-phenanthroline)iron(II) 7.15” Tris(S-hydroxy-l.lO-phenanthroline)iron(BJ -tris(4-hydroxy-l,LO-pheenanthroline)iron(B) 6.82” T~(ehydmxy-l,lO-phenanthrotin~)ironO -tris(S-hydroxy-l,lO-phenanthroline)iron0 6.24” Congo Red 5.80”’ Tris(~hydroxy-l,lO_phenanthroIine)iron(21) 5.45” Evans blue 5.35”’ Methyl Blue 3.60”’ Fast green FCF (major component) 3.05**+ Patent blue V 3.co”’

* Ref. ** Ref. -** Ref. 0 Ref.

27. 26. 25. 10.

7.58 f 0.02 7.22 & 0.05 6.18 f 0.02 5.45 1_ 0.02 5.35 4.95 + 0.02

subcelldm

‘8

Aconitasc”5

Acid rib&uclcas$~

Acid,protcnrnP

’

Acid phosl~hntase!l Acid~phosplintase~~

,,,’

Acctyl transfws~‘A~” Acctyl”iransfcrnst? Bta ’ Acctyl,trausfcrnscBI”’ Acicl~lgalnctosidas~3q~*0

4

liver str. 408 str. 8325

lhytiius(nucl.) thymus (nucl.) thymus (nucl.) intestine

testis testis cpididymis

cytosol mitoch. liver cyto. liver mitoch. liver cyto, liver mitoch. brain cyto. bruin mitoch.

Lymphosnrcoma D1798 heart pig

chitkwsis

S. attrrrts S. sirms Rlrizoprrs

rat

‘rat , rat mt rat

Slapit_viococctts wrests

‘,.‘gInidn&7

: :‘~-*cciyi’murclmyl~L-alanine

frtrcrlgettti

Sclerothiu

jack bermmeal shocp rmn mm

/I-N-AcctyfgkrcoSnminidasc31

,.’

rat

ox

AcctoncctjMoA tlri&se30

Acctoncctyl-CoAthiolasP

rat

Au%oncctyl-f?oAtliiolasc30

/M%‘~clyl glucosaminidasd”J’ /I-N-Acctylglucosurninidas+’ NWAcctyl hcxosnminidas.P

‘.

:

yciit

Aceloacetyl-CoAtl~iolase2”J9

lOCOtiOl1

19000 GGOOO

35000

100000

30000 99000 110000 92000 95000

140000 140000

141000 100000

1.4*10* 0.65010’

...-..__ No. M. W. . ._. ,.. . _ . .._-_. .-- .-.---. ..-..--.---.--.~.---...- . --....___ ,_, _..__.__.._. .. .._._,..._- . . ._.....__ __,_,.,_,. __._ ___..___.

iso-

idwe

5.3 tl.5”,8.1,7.9

5.2*,5.9

4.75 ‘4,75 4.2”,4,G,%I*, 61, 8,O 7,7, 4,s ,’ 9.58*,8.40 9.47’, 8.42

5.90

9.7

3.7G 4.8 6.0, 6.3 6,45,5.85*,5,95* 7.15,7.0s*,

5.3 7.8 4.8 8.4 52 7.8 5.1 8.3

1 3

‘2 2’ 2

1 1. 1

n,S. ,: ! n,f3.

‘, ‘4 n.s. ‘ll& f’ : ,”

,n*s. r-i&*, :n,R, ‘:,’

cllzynlcs (“C)

M.W. VALUES OF PROTEINS :,ocCl.=;’Acclimated,chloro. = chloroplust,,cyto, = cytqplosm, lyso. = lysosome,micro, = microsome,mitoch. = mitoclrondria,n.g, = not Bivcn,nucl, = n~~1cu~,pcrox. = peroxisoinc,r.t. = room tempcfnturc,s.p,c. - singlepolypcptidc chin and str. = strain. ..~__‘__i’_ ._^..__. . (--.-_. ..._.._...._” _-..__.__.-._ .._....... . ,.-.... ..._.-__..-..__. _..,... _^,..,-____..._ .._. __.__...“._ .._.._.. _ .._..___- .._.-._.. ___,_ ,.._,.__._.-__.-.._.,- ..._.. -- . .-..--_._ .-.._.. Proteiy AYowce M. W. Orgm and/or No, of Tcq.y Slrbutrit PI

pl:AND

TABLE 2

‘.

a!

-_--_.

E. coli

lNllnal~

._I ___. .__.-_---.- .-----.--I--

L-Amino acid oxidasc”~‘*

human human

Alknlincphosphatasds Alknlincphosphatase66 Alkalinepl~osphatasc6G~“7 Alkaline phosphatusP Alkaline pl~osphatwd~J~

cillf

ycnst

_---

rabbit

Aldosc rcductw?”

pigcon

Aldokw?’

rat

muscle

hen

AldolusP

AldolnsP

muscle

rat horse ycnst humun

Alcohol dchydrogcnw?’ Aldchydcdchydrogcnnscs9 Aldolasc60~*’ Aldolasc61

vclloll~

plnccntfl kidney intestine liver

muscle

n~usclc

muscle

liver liver

plnsmn serum liver

human horse

Esclrcriclti~ call ox

Adcnylntckinasc5* Albun$PJ’ Albumin”Js Alcohol clchydrogcnnsc56~5T

liver

fibroblnst fibroblnst crytbrocyte

heart cyto. hcurt mitoch.

rat

mow humnn humiin

sit3

pig

Adcnyhltc kinases0*,51

Adcnosincdcnminnsc4g

Adcninc phosphoribosyltmnsfcrns3~7~1B

Aconltate liydrntas~~~

1

4

4

4

4

2 4 2 4

2

2

3

135000

80000

140000

2

2

2

1 11GOOO 2

GIOOO

IGO000

160000

160000

lGOoO0

GE000 245000 8OMO lGOoo0

46000 27000 G9ODO G9ooo 80000

34000 32000

-_

_

4.G 4.3.4.8,S.I) 4.4 3.9 S.OG, 5.17,5,20, S.2C, 5.38 (5.2-8.4)5.60*, 5.71*,5.87”

.-

I8

5

5s I 4.48 I 4,70,4.83*,4.94, ‘5.06 7.5, 8,0 495 5.18,5.07,4.98 s,a5* fl,O8,8.28,8.51, 12 8,7*,9.29” 9.7 1. LOS”,4.80 2 5.1, 5.2*,5.3 3 9.13,9.30*,9.4”, 9.59*,9.73 5 9.87,9.96*,lO.O*, 5 10.06”,lo,11 9.9,9,97”, lO.O”, 10,09h,10.15 5 9.1,9.27,9.42’, 5 9.57*,9.71 9.1,9.25,9.39*, 5 9.53”,9.70” 5.05 1

.__. -._____.-. ___I-.

70000

40000

69000

23000 36600 58000

4OMO

40000

40000

40000

39000 57000 40000 40000

s.p,c. 41000

S&C.

S&W.

23000

11000

5,4 7,4

0

n,g. n-g. n.g. n,g.

n,g.

4

4

4

4

4

n,g, 0 n,g, n,g.

n,g. n,g, n,g, 25 n.g,

r.t,

r.t.

0

rnt red kangwoo red kantwoo

A~yis~iipdninsee~ ArylsulphnttisdAa6 ArylsulbhatascDa6 L~Aspnmginnsd7J’~

AspurtnlcnminotrunsfcmscN, sheep &p&tic ~wnialdehydc dchydrogcnrtsb9g” ycrlst AqinrtoliinascL-homoscrinc dcbydrogcuiiscP6 E, co/i ,’ Biotincnrboxyl-cnrricr,protcinD7 E. cufi ,, ?IromclingB Aaanas cot~Iosas

L-AspnrrrginescBg~90 Il. coil ASpinmgi?a,synthetasc9’ II. coii A!pnrtn\e nn~inotr~nsfcrnsc9z~gJ~ pig

Erwirtia caroto. ifora

Psei~donoaas acriiginosa

Arylsulphntn&” ‘,

’

guincn pig

li~ttOlVlltt

Chysosporim

Fonrc.vprrrrosrrs

Aspcrgiiius aiger Sterem saagaiaakrrtlflrr

Arylcstcrascn3

At-y!/I-glucosidnsP ‘,Aryl fl-glucosidawP

Aryl /3-glucosidas?*

Aryl ~-glucbsidascR’~a*

Cot~iortrix

ArgininccstcmscUO

loticiflctlls

Scrratia ararcesceas

Anthrnnilutc synthotnsd”~7D

--..

humnn human mt guincn pig

.__._..._.__.... _____-

____

___

_.._ ,..._._......_-_-__.- __.--..-

.._.......... _..___--__-.--:__.-_-.L.-.-_.

stem

str. K.12

liver

henrt

kidney liver liver

cerebral cortex

venom

sl~Mlldar

360000 45000 22000

15GOOO

89000

135000 133000 80000 92500

100000 45000

50000 180000, 78000

50000 50000

30000 50000

M. W.

22500

1 1

4.5 9.7

1

6.1 86000

5’

4mO

:

1

1:

1’

2 2’ 2 1

3 ,I

5;53,5.69”

5.35 5.5 5.35,5.41,5:43,

.8.00

4.85*, 4.9’ 4.4,6.2 5.1,5.4 7.0

2

3

2 2

1 ,’ 2

5.35; 5.56,5,75 6.17

33000

32500

GO000

5.1*, 58’

4.22,4.38,4.44

4.00,4.08 4.08,4.17

9.1 4.21,4,43’

kg. .25

n.g,

,, kg. Jig.’

25

‘,

‘.’

_’

,’ ‘,’

‘I

,)/,

$ ‘,.‘...,, .’ 8,’

,“‘,

: 1,:,.:iz ,’ : ., g”

.’

‘, I-1’ ,’ ‘, Q

1,

7 ‘, ,,P ,, ” ‘, , E, ,Q.: : :; 1, ,,

”

;

’

w-

I.. ,’ ‘, .;.,,

:

11.g.. ‘,I;’

,5

r.t,’

n.g: n.g:

n.6. n.6.’

“,&

4

4 4

‘4

n.g.

No. J Tmjm Silbllnir PI _.___ __...___ ._... iso- atare No. M.W. arz}wles___.-.-_..I (“C) location ._..._ _____ ._...-___..._ ___ __... --__._.. . ___.__ .._..._ - .._... -_.--.-....._., -- _..._.- _____.___ 1’ 4 parotid 55000 5.95 snliva 55000 G.4,6.1,5.6,5.3 4 22 8.77”, 8.95* ptg. pancreas 56000 s,p.c. 2 52000 8.4 1 ‘jLl() pancreas 2100 4.6 1 n,g. 150000 2 2 60000

.,..._...._.__._... __..__ _-.....,-... -, ..__.__._._..--_ -.-.-_.__--.-Sorrrcc Organ aadjor

a-AmylnsolJJ~ a-Amylesk? a-Amylusc76 $-Amylaso”

__L.-____.._.._.__..

_--__._______.___ Proteia

TAIM! 2 (coarinued)

Virisvill~b7l

Catcchol oxidnsc”’(tyrosinnsc) CnthcpsinB’lll Ccllulasc”~

Ccrnmidetril~cxosidase115 Ccrcbrocuprcin”” -- . - ..___..._. . ._._ -__- .

Ccllulnsc~’ dellulnsc(C’coniponent)114

hum;m humnn human pigeon mouse

Cnmitinc occlyltransfernse109 Carnitincncctyltrnnsfcrase’OY CnrnitincncetyltrawfcrnscloY Cnrnitincwlyltransfcrnse’“~ CtaIlilEiC”~

o/l/Ioslis

..--

human liumnii _..

Tricllorlerrlla ftorliu~ii

Jbms

Cllrysosporilwl Ii~Ilorflltl Aspcr~4llrs rliget 8. smlpriwlcll. I lll~l

humrin

rnbbit

Cnrnitincncetyltransferntdo9

plnsmn brain

liver

muscle liver pcrox, liver cyto.

b~ilill

2

3

95000 4 35700 -. _... - .--.

25500

92000

liver micro. liver micro. liver micro. liver heart, brain, n1usclc ntlreanl lienrt

crythrocyte colonic 1nuc0s:t crythrocytc

humnn guinea,pig pig ox mt rat rnt beef

I’se/Itlorlrorlua sllrlzeri

150000 70000 I77000 55000

crythrocyte

bull shark

Carbonic mhydrmclOO Cnrbonicenhydrasc*O’ (A B C F,D, G, M,M, N, 0, P, ?,‘U:X) ’ Carbonic nn11ydrasc~~~ Carbonic nnl~ydrasc103 Cnrbonicnnhydrnsclu103JD” CnrboxylcstcrnscE’1f15 CarboxylcstcrascEJO$ CnrboxylesternseE’10a Carboxylcstaaso’“’ CarboxypcptitlaseG”O”

1500000 38000 254OQ29700 30000 30375

brain

human

ButyrylcbolincstcmseP

-_._ -

22000

s.p.c.

46000

GISOO s.p.c.

1

..

--.

5

4 4

4 4

n.g. n.g.

6 G

n.g.

IL&

n,g. n.g. n.g.

___-_

’

(Cot~rit~acd on p, JO)

1 n,g, 1 n.g. _^___._-_ _---__-_-

2

I 2

3.58 3.9,4.2* 3.8,3.95* 3.0 4.74

5 3

3 3 3 3 3 1 3 3 6

4

1 1

IL&

1

22 n.g. Lg. n-g. n.g.

I 1 I

n.g. n.g.

kg.

22

22

14 2

6.1,6,7, 7,9” 6.0,6.8,7.4” 6.I, G.7,7,6* 6.1,6,6,7.5* 7.0,5.85*,7.8* 6.7 8.0,8.2*, 8.5 4.7”,4.9’, 5,I (4,5-5.5)S,Ok 4.27,4.43^,4.7* 5.05”,5.53 3.9,4.2,4.52*

7.1*

(4.85-8-12) 5*2,7/I 7.3 5.89 5.7 6.6 5.65 5.5

1

6

(5.6-8.0) 4.5

IL5

(5.6-7.0)

-_

_-

___

.

.

-.

.

.

C/ostric(irrrtr

humnn Congulntionfnctor VIP Cobnlophilin(Vitamin&-binding human protcin)*arr Cobnlophilin(VitaminBri_binding human protein)‘*” I.2 coli ColicinEP 8. coli ColicinE*3u Co-lipnse~31 Pi& jnck bean ConcnnavnlinA”2J33 Crcntinepl~ospl~o~innseb7~1R’ rnbbit CrotoxirP rattle snake a-Crystnllin’“b-‘3” cow

perfiitrwhv

ClostridiopeptidnscB126

OX

phtessa

s.p.c. s.p*c.

lens

venom

pancrcfls

17500 4OObo s.p.c. s,p.c. 2lSOO

S.p.C.

s.p.c.

amnioticfluid

59300 62400 62000 9G50 71000 4 81000 2 9000 12000 2,7.10”(a,) 620000(aI)

s,p.c.

44700

25000 23600 25850

salivn

serum

pancrens pnncreas pnncrens liver (cold nccl.) liver (warmaccl,)

muscle pnncrens

3,0, 3.3,3.7*,3,9 7,41,7*rj3* 6,64 5,o 4,5,4.7,5,05*, 5.5 6.6, 6.7,6,9 3.7 8,6 4,5,4.85*

(4.5-5)

485 5.6

8,5 8,8,9.2,9.6’ 8.97 4,8,8.7’ 5,76 5.05

5.3,6,9,7.5 8.38,8,76”

6.6 6.8 7.5,7.8,8.3* 7.0,7.6,8.4*

Pllwrorrectl~*~

6.5

21600

.._.

pigeon guineapig rat cnt brain brain brnin brain

locatior1 _.___. __.--.. _.._

_-_______-I_

4 2 1 1 4 3 I 1 2

6

2 1 1

1

3

1

3 3

1.

1 I

n-g. 4-6 4-6 46 4-6

No.of Temper_--. __. ._.. PI iSOattrrc No. M.W. arzyrnes (“Cl ___-_ -.__- ._._._---.__. -._... . ._ ______.c^--- __^.~

ccreus

LlaCiIilIS

ChymotrypsinogcnAm ChymotrypsinogenA75J14 Chyn~otrypsinogen77 Citratesynthasc’*”

-.

sabcellalar

-- .-_- .._-. - -.__._-_--- _...,_-I.---~--._-~------.--~ Organ ad/or M.W. Subiodt

Psel~rfoIrrorras ner&rosn beef ox guineapig trout

cr-Cl~yniotrypsin’20~1~’ 6-Chymotrypsinl*~

-

-__---_

Soarce

- -.. --

Cholinencetyltransferase*‘8 Cholineacelyltransferasen” Cholineacetyltransfcrflse”” Cholh~cacctyltransfernsel’B Cholinesternseng

CereolysiP

I

Proteill

TABLE 2 (carrtiaae(I) .-.--__ _,..-._--.__-__ z

b-555’43 b5 rcductase’“’ c115 P cl”

DDT dchydrocl~lorinusc’5*~‘~3 Dcoxyribonucleasc’54

Cytochrome c pcroxidaf@

Cytochromc c&49

Cytochromc c350’la

Cytochrol~c Cytochromc Cytochromc Cytochromc Cytochromc

Cyclic AMP dopcndcnt protein kinnsP’ Cyclic nuclcotidc phosphodicstcrnnfiP Cystathionc eynthnsc141*L4Z

vitlelnndii

Azolohclet

ilersorlli

Spirililln~

SphCrO#&/lfl

UM~~O

IlCCf

-

-_---___-___

liver Inrvnc liver hcnrt hcurt

liver

PC0 rat

chicken house fly cnlf horse

liver

4.12*, 4.35 5.1, 5.35*, 5.76’ --_ _-__I__-

60000 __.--__

6.5,6.7* 6.3,6.0,7.4* 2.5*, 5.0,6,2,8.5, 10.1”

9,86 4.63 (rcduccd) 5.17 (oxidized) 4.07 (reduced) 4.2C (oxidized) 4,55

9.4

4.24*, 4.28*, 4.32 (i-8 9,0,9.4* 10.37,10.57, 10.80*

6.0

4.3,4.6,4.8 5.S

7,6,8.2”, 8.5*

7.25,7,35,7.Q, 7.80

(5.95-7.0) 6,55* 6.80”, 7.0”

71000

3OOoo

s.p.c.

45000

12oooo

s.p.c.

S.p.C. s,p.c.

s.p.c.

12000

10800 12000

12500

S.p*C.

12200

51000 73000 s.p.c. s,p.c,

4

2 2

125000 11300 43000

350000 #?5OOoO

20500

lens

cow

rot

27500

lens

cow

3

2

5

2 3

1

3 I

3

4

10

-(Continrrecl on py 12)

4

n.g,

4

‘, I .‘, r’,‘, n, , ,,’

.-.__._ -_----_

Ferritin’7! iriFctoprotcin*77 Fibrino&cn17a

‘8

Fcrritii?~a’~

._--_..I._._..ProtciIi ,,

human rabbit

‘rat

rnbbit

liver foetus plasmn

liver 72000

5.45,5.50,5.55

5.50,s.gs ,4*98, s.od”,5.15;’ 5,18 5.16;5.24*, 5.3 &7B”, 5,2

2 3

4’ ii

5.

,:.

‘,

25’ ;,:. 11.g. ;

n,g. 3)

n;g.,.

..‘Q

,, ;

,’g :, ‘: $ ‘,” 0 ,g

--.--..c. . .--...-......._... ._.,I_. -..-......-.-... A...-.....----_.- _.__I._ ..______ -.. .-_-.-.__..-.-___.._ ______.__ --_-___-...-I.. Sorrrce No.‘of TetujerOrgan atrti/or M. W. px Sir@nit .’ “_~_____._ isoatrrrc ~srrbcellrrlar No. M. W. locatiorr enzyme (“C) ..___._-_*-_.._-__-.-_.~.~_-.___._.-.-_.._.-_----_ ._,.. ._. .._ -_..--____~..__.___.L_ ..._...._1_..__ --____-_.-_-._--. N,O-Dincctyl murdminidAse’s7 Chalaropsis 20 ” 19000 7.53 ‘1 s.p.c. ‘, DincetylreductAse’jn Aerobacter 0,’ ‘,. aerogem 100000 4 25000 5.75;5.9,6.55*,6.R” 4 DNApoljmcqw$3 Drosopkila ‘. wchtogaste~ S.3*,5.8’,6.3*,7,5 ‘4 embryos ~NA polyirrcrnse P & coli I ::;: 5.2 o,., I’ Eqdonuc!eiw?oo ox plasma I 38000 7.3 Endbnuclens’c*61 3 15 ‘, E coli 4.3”,6.1l, 8.5 EndonuClcnse’6* Micrococcrrs 13500 4.8*,9.0* 2, 25 ,, ., lysodeikticrrs El101ASd~J6~ ycast 2 88000 5.4,5.6*,6.0,6.6,. 44000 ,, 6.7*,6.1);7.1 7 nd.?., EnierotoxinAl”’ S. amws 27800 G.64,7.26”, 7.68”, 5.p.c. 8.14 ‘i ‘4 Entcrotoxin& S. amus 24soo 7;85,7.!j3,8.i5*, ,’ ’ .’ ill,,, .24’ ,,, ,. ,. ,.’ 4 8S5” ,,4:’ Entcro!oxinWdfi S, aweus 24500 8.5,9.05*,9:4’;q.56 4 Epidcrmoly&toxirP S,~aurelrs 25000 s.p.c. 6,2;7.05* ,2 n.g.(, ,I ., s, : ErAbutoxin~C160 Loticaurla ,. I, ., .’ siw~fasciata venom 7000 ‘,,‘$ s,p.c. :;y ” n.g., ’ 1 ~rythroagglutinin’bD red kidneybenn 150000 ? 37000 I n.g. ” ” ,: 0, Et$h~‘bcri~~ri~~170’ Lurrrbricrrs blood 3450000 I48 23230 5:os 20 .I Elythrocuprcin116~11’ hlm~An crythrocylc 33600 ,) ,4.75 ‘, 1 Ii.& P Esterasci~o ‘7“’ beef liver ssqoo 5.5 1 iI& ” : Fcr~itW2J7” horse Spleen 44oopo 24 18500 (4.27-4.57) 4.27”; ‘_ “,,c ; ;r;l,, g., ‘20 .‘,::,, ! ‘, 4.35*,4.40” F&i$n~7’ ,, humin, liver s.i9,5.35,5.45*,

TAIU$ 2 (conthxl)

rat

,1igct

crass~

Aupergilllis

Ncrrrosph Nicoriarra glritirrosri

Aspcrgill~rsl&w

pig

Faraliiiwtics canllcllafica &+~a gracilis

Aspl!rgilll~sni&vr

/I-GlucosidnscsZ /I-GlucosidasP

---

--

sl1eep

--__

brain --.--_

kidney (mitoch.)

beef

IL coli Achromobncternceae

ccl1culture kidney prcputinls

parslcy ml rat

-_--.-

GlucosinolasP Glucosyl truusfcrnso’g’ 11.Glucuronidasd” /I-Glucuronidascto3 L-Glutamatc.phenylpyruvatc L\n~inotrn11sfcrasc19” L-Glutaminasc’g5 Glutuminnse-aspnrnginnsc196

/I-GlucosidnscAt90

Clirisosporiirrn Ii,qrrorrrra &xq?ilhs wcr~rli Sitlapis aIOa

kidney

pi6

/I-n-GlucosidosP'

llIm+~~

crylhrocytc

hypophysis brcnst liver gill hypodcrmis chloro. cyto. heart

hulllall

Glucose-G-phosphntc dchydrogCatrdkla rdlilis nuse~R’ Glucose-G-phosphnte dehydroge-

Ructos&l,6-diphosphntascI nnd II’@’ Fructose diphosphntenldolnsP

chicken

Fructos~1,6-diphpsphataso’80 chicken

(FSH)“~

Folliclestimulatinghormonc

138000

280000

50000

170000

soooo

110000

45000

96000

191ouO

4

4

2

4

_.

35000

75000

S.p.C.

55000

48500

‘1 9

8.3 4.65, 5.25, .s.45* 5.75*, 6.20

. __.-._-,____.,._._. _.._ ... (Cor~riwYl f?fl ip, I?/)

1 I.

9.8 4.2

________.

: 1

3.8 s.o,s.s5 5.0 4.G, 6.7 615

h

I

; 1

5,79,5.34,6.11, GJV, 7.04” 4,3*, 5.1 4.46 4.38

3

5.50, 5.87,6,54’

1

4,87

II

1

:. 2 1

,t

2 1 2

/

;:9-8.2) 7.58”, 7.73”, 7.90” 4,1,4.5” 4.3 4.78”, 5882

7.5, 5.3h 7.2”, 5.4 4,6

8.1

2.8 8.6

Source

Gunninephosphorybosyl tnnsfcmscza4 GulonoIncton~sdO” HacmoglobinAzo6J07 HncmoglobinCio”*07 HncmoglobinSzoEJo7 I,H$moglobin FP6J07 HnemqfllobinFJooJo7 HacmoglobinA (a-ckain)zo0 HwcmoglobinS (/?~hnin)Zon Hflc’moglobinzog a-Hscmolysin(a-toxin)21o @Iacmolysin211~ 8.Hwmolysin(f?.!ysin)2*L*a’2 I+Icracrytrin2’3

ul~Glycoprotcin’Oz GSM tran&nsczoS ‘,

S. aureus S. aureus Demiroslomum pyroides +

rut humnn humnn human humnn human humnn human hnrp seal S. aureus

Al?.con

bull frog sheep rat mouse house fly cockronch gross grub

_I----._LrClutarnylcyclotrnnsfcr~sclg~ human Glutnthioncopoxidctmnsfcrasd9~ rnt Glutnthionc-S-trnnsfernsc19g mt I Glycernldcllydc-3”phosphate dchydrogcnasc9s~200 ycnst Glyceraldehydc-3qhosphritc rabbit dchydrogcnnsczol t-G!ycerol.3-phosphntcdchydrorabbit gonrw60

--__.-_________Proteln

TABLE 2 (conhued)

107000

74000

44000

42000 64SOO 64500 64500 64500 64500

8

. *

4 4 4 4 4

2

66000 78000 2OooOo

ndiposc tissue skeletnlmuscle serum liver liver liver

35000

4

144700

13000

pl

6.71

1

2 3-4 2 I

1 1 1 1 1 1 1 1 1

n,8.

4 4 4

9

8 15

LJ $ $

I’ 1!I

,

,’

z c)

;

0. 4 4 n.g.

__

F

iot.

4 4 r.t. r.t. r.t.

n.g. n.g. 9 n.g. n.g. n.g. w. n.8, n.g. 1 I 1

6.35 G.45 4.5 7.1,9.5 7.6,8.0”, 8.6”,9.4 8.2*,9.8 !&IS”,5.9,6.8 4.5,6.6”, 8.5 4.5,5.2*, 8.8 5.5 5.20 6.95 7.40 7.25 (1.90 7.15 8.12 7.08 7.06”,8.04 5.0,7.0,8,5* 3.5,9.5* 9.6

n.6.

2

8.32,8.52*

2 4 2 3 3 3

n,g,

________-_-...____ n,g. 2 4 1 n,g. 2

,__-___-__-.__ No, of Temper- I aturc iUOenzymes ( ’ C)

1

---..-

6.25

4.OG*,4.25 7.14 G.9*,8.1*

--PC_

-

s,p,c. lGOO0 ’ 16000 lGOO0 16000 1GOoo 16000 l#OO

37500 s.p.c.

36000

24000

14cQOO 4

kidney crythrocytcs crythrocytcs crythrocytcs foctus roctus crythrocytcs crythrocytcs blood . str. V8 str. RI str. Rl

M.W.

I____ 2

No

,31rb1rrrit _.__ -___-

40000 40000

M. W.

liver, muscle

brain liver liver

-.---___-

Orgun anrll~ subcellular lOCQ!iOl~

_-._-

Polyporw

LnccnscP

I----I-

fl-Lnctoglobulina7*R3* &LnctoglobulinA235 /I-LnctoglobulinB23J

Lsctntc dchydrogcnnsc60 Lactotc dchydrogcnaso””

Lnctnsc2~z Lnctntc clchydrogcnaso2’J

__--_.-

-------__

i3acillus steurollkwophilrrs cow cow cow

rat chincsc hamster rabbit

S. aurm P-Lnctamasc(pcnnicillinosc)z3n~*31

versicolo~

crnssa rseridoalorras putida Mycohacteriwt~ plrlei Polyporrrs vcrsicolor

bukcr’syeast Newosportr

----

milk milk milk -.

str. 408 str, 8325 intcstino skclctnl muscle

._--_----

crythrocytcs

human bmf pi6 yeast

crassu

hcnrt

str. Ml8 str. V8

liver

pig

S. amws

humnn ycnst S. aureus

2-Kcto-3.dcox~G-pllasphogC conatc nldolnscP” a~Ketoglutnmtc-glyoxylnte cnrb01ign6c117 LnccnsoAateJIP

Isocitntc dchydrogcnnsd” Isocitrntc lynsdz5

InvcrtwP

Hcprltocuprein’*6 Hc~okinasc~14~*‘s HynluronutcIynsfP Hynhwonntclyux? GHydroxyacyl cowymc A dehydrogcnnSc21L219 Hypo~nnthinc-gunninophosphoribosyltransfcrascZzo Insulin7J**a1 Insulinn7 lnvcrtnsa”*

___._

135000 35000

62000

73300

.-______

4 2

3

_

---.

34000 17500

24000

40000

51500

4

2lOooo IO

34000 5730

2 2

Gmoo 1146G

375000

31000

51000

2

2

.-

..__

-.-

__.

_..

.

5.5 5,1,5.26*, 5.34* 5.13 5.23

8.3,8.4,8.55*

.._-

-_

.--

2

1

5.6 3.01,3.27 5.70*, 5.9,6.13*, 6.26, 6.3G,G.S6 8.38,9.25* 8.48,9.55” 4.4 5.7

1

1

I

I

_,__

_.

.__

25 25

r.t.

n&L

IL&

4

n,g.

n,g.

n,g.

n-g,

4 n,g.

5 4 r.t.

4

_.._.

_

(C’ontlrr~~cdon p. 16)

IO

1 I

3

1

4.7

5.5

5.5

;tL 4) 4.02*, 4.24* 478

5.66, 5.82,6.00 5.72

8,95

4,76 4.7 7,4,7,9” 6.4: 8.2”

root 110dules

Lllpill serrltrle~la

kidney bean kidney bcrrn yeast

, LcgBacmoglobin237~

,LcucoaRfilutitiinZ~~ Lcu~oagglutinin’aD Loucyl-t-RNAsynthetbse’3Y Lipnsdqo

':

,.

NCIll?S

guitica pig

gunw pig

fircRy

pig

>

a-Mnnnosidns~5S

Mhnriosidesce2

,/I,

Marinannsd*

‘I

muscle

serum

egg mcmbrunc

hypophysis

It&t

puncrens pancrens heart

soybean

Clwysosporii~~~r I~griorrrst Aspi@h rdger

St. snrr~l4illolcIltr~I~t FootesNII~IOSIIS

Aspcrgilhs t@w

L&ink&g hormone (LI~I)a4dJso rnt LysinzfL’ Tegh pjkifferi LysdzymcZ5Z hum Meticenzymd? kcaris suum .’:&Worry1 CoA-ACPtransncylnSc*~’E. &J/I

L&e~~~c2'8

~Lipoyldchy~lrog,el~~~s~~47 ” ,’ ‘,

Lipoomidpdehydrogcnnse2~1 pig Lipbxydcsti(lipoxyge~~~s~)*~~~~*~ soybcnn : Lipdxygcnasoz*3J44 soybenn Lipoxygens&?4s p&t Liljd~y$ww3Z46 Pea

.Lipnie 277

,‘Lipnsc1177

CovJ’rreh?crcrirc/tl

root nodules

milk

cow

Lnctoporoxidnsc236 ),,

175000

248000 36600

100000 31000 8800

100000 108000 108000 70000 70000

20000 18000 126000 140000 120000

85000

‘.

4

2 2

2 2

4 4 2 .,

5.7, $+I”

_‘Y

4,5,4,75”

4.68

4.11

3.5g 3,9”, 4.2

‘3,9!i

’

‘.

56, 60, G-S”,6.8’ ,5,G5 5.68, G.15,6.26 5.80”,5,82” 5,85, 5.92,5.97, 6.01, GOG,6.17 5.9,G.L 6.3,6.6, G,g*,7.0,7.2

3.8 5.1 8,l

9,0* 7,9 10.0*,1i:o GGSOO G,63 s.p.c. 4.G5

15500

‘50000

54000 54000

49700

80000 663000

9.16,9.32,9.49, g&8*,9.7*,9,80” 5.QB;5.13 s.p.c. s,p.c. 5,00,5.05 31000 5,l 35000 5.0 GOOW) 4,9

‘1 2

‘.l

,2

1 1’

7 2, 4 ,l 2’:..4 ‘1 1

25

G

): ,:”

:

..(

‘4’ il.g,

4’:

4

‘n.g. .4 ,‘, ,4

,.;

,,

l,‘,

,“,;.,I

0,

5 ,,“,$..’ .Q ‘, ,g.

:cj

,P “1, Iif& ;“~~,cl. n.g.. ,, ‘. do,: ,’ 5, I’:,, s ‘,. 8,,; I’!,$

Y,

”

‘, ,;,; ‘,,, ‘, ‘,

,,

.,,,,

:

,, ,,:I:

‘,‘:>

‘n.g. : ,’ n.g.” ;,‘,

,:

11.g: :

‘25

ng.

Jig.

y$ -

n.g. 4 1 3 2

1

.I

1

” :’

n.6: n.g,’

:

,‘.

“,‘,

,’ ”

n,g, n*g* 11.g.’ ‘ne. ,~ ,:

i 2 ,2 1

,’

,, I,, ..,’ ,’ )II : at ,- _.,....__.. -.. ;- ..--- _.-..._-.-...-.._^...______I_...._... ,.__. ..- ..__.. - _..... _.- -.-.__. _-...-- ..-_.-.__-._.. . Orgarinrd/or No. if Tetnpcr-, “’ :’ M.W. sIl6illlit PI, _..I_ ___.-srrbcellthr iso,mre No. M.W. locdorr errzynlcs (“C) ,’ :‘,, ,I .._.... _..-.._-_. - .-___-._ ...-__-_______ _-._.. . . .-..._. . ..- -...-._-...---..- _.-_ _-..-.- . .-..-.-_.--._ . ..____. ._. ..__,.,,__ _..__... _-._. _._. _.._____ _.,.__,___.,___,_-.____ __I_ .,,._._- _.._1___^_,

TABI& 2 (cowhrred) .._--.___-__.-k_ . _.___-____.__.___ . . .. . ,_...__ Aotebr (’ Source

13SOoO 2 151000 2 33000 2GOOO

rapeseed whitemustnrd

Rlrorlospirillw~ rdtrttrt~

MyrosinnscCzar

NADl-Idchydrogenascza2

lnflucnznvirus

Pncumococcus rabbit

spinach

Ncuramh~idnsc26u Nculrat pro1ca%P9

Nitrate rcductasc”O Nitrogcnasd7’

Kldtsidlrr ptictttttonicre

Viitrioclrolcruc Cl.pcr$itigetrs

Ncrvc growth fact~r~~‘J~~ Ncuraminidase266 Ncuruminidasc26n NcuraminidasP7

mouse

NADDisocitratcdchydrogcnasP rainbowtrout

__

__

potymorphonuctcnr tcucocytcs (lyso.)

Azlt9S7

liver(2”) liver (I?‘) salivaryglnnd

G6Roo

24M)oo 218000

G9RoO

200000

26500

2 2 2

4

2

I 1

Acnnthnmocbn

Myosinzbo

sperm sperm

musctc

1

180000

whale

Wlll.llC

muscle musctc

muscle

17500 17500 17500 17500

horst: horse hoac r ox

MyoglobhP Myogtobin6 Myoglobinn7 MyoglobirP9 Myoglobiu’” Myoglobid7

musctc

pccthl livol

tomnto hog horse

Melhytcstcrasd5 Mcvalouickina!# MyoglobhP

100000 200000 26300 98000 17500

Brrcill~~s brevis

Mathlonyt1-RNAsynthctasP

__. .

50000 60000 34600

4.0*, 5.9

3.5,4,9” 5.0 -.

140000 lGW0 14000 GSOOO 4.96,4.99,5.OG” 5.08 62000 4.i.I0*,4.91 4.50 5.75 S-72*,6.9 13200 4.50.9.30” 4.80 4.95 50000 5.2, 5.35,5.5*, 5.8*, 6.2, G.5 s,p.c. 4.9 4.2*,4.8,5.2”, 6.3, 7.0, &2,9.1

s.p.c. s.p.c. s,p.c.

5.P.C.

s.p.c.

4.4 5,0* 8.4 4.7 6.47, G.53,6.60, 6.79, 683,692, 7.17* 6.76,7.tB G.8,6,8G,7.21,7.76 6,8, 7,0,7.1: 7.5” G,SG,6.74,7,01* 7.52,7.79 7.1, 7.4,7,6,7.68*, 8.01* 8.0”

f Corlrirllrcclor1 p. 18)

1

6

5 3

n,g.

3

-_ ._.__. -_-._____

^_..____--.::_..__-.-.__.Sottrce ,I

ox rat rnt

OxoncylCQAthiokcz7@

:

:

E. COB

sugnr beet

pi6

horscrndish horscrudish

hog

;hos;holypuso A2p’

Viper0rrrsscllii

Pho~phoglrr~omutnsclOO rabbit G~Phospho~luconnte dchydrogcn- Netthporn &$C’P” crwa Phosphoglucoscisonwnscz9~ humrm Phospholypnsc,A293 honey bee Pho@holypnscAaPl NRJrrttaja

._ap-$D+W

I’~osphoncctylglucosni$nc mlitn,sC26” ,’ I Phd;spliodic~tcrascz~7 Phosphoenglpyruvntecnrboxyl.

Peroxidndn3 @o~idcsc~~~J’~

&qjinl’&

.. ..-.--__._ Orguttand/or sttbcclltdat

6.8,7.3, 8.3

;.

venom

erythrocytc venom venom

muscle

subninxillnry gland lenves

gnstricjuice root

99600 s,p,c. 57ti 62000 19500

liSOQ0 2 125000 2 40000 2 850020200 l5OOO23800

27000

37800

33000

4

402000 64900

110000

33000 45900 40000

,I2300

~IUECh?

3

16DOOO 6 11900

80000

108000

1

liver (mitoch.) liver (mitoch,) liver muscle

w3

liver liver liver

29000 132000 1

2,

‘1 J ‘2 1.

6

”

9.90”

(4.60-5.66)4.95* (4.62-9.90)9.52”,

4,93,5.50* 9,0,9.1,9.2’ 10.5

G.cP

4.92

4.8’ 3085

7

11

,’ 3

,’ 1

I

”

4, ,, 400,fI.8, > 11 (3,9-O)6.1*,,G,G*, 20 1 7.2*

6.25*,6.50,6$5, ‘6.23*,6.50,6.73” 5.7”,6.3,6.7* 6.95,8.15* 5.5 ‘, 4.45 4.65 2.86*,2.94

6.19,6.36,6.44, 649 5:62: 659 5:78;,677 ;.o;, 6,’ * :’

G&7.1* 5.38 3,2*,4.4

Il.&~

n.g. I’

.I

r.t, ,, kg.

‘.

20

n.g.

.4. I;.t;

lit.

20.

22

()

6’.

n.g.

‘,

,,

‘. 1

‘,,‘:

,,

5.

:” ,, : ” ,:

;g 8

‘, :‘:’ :#‘, :( : “‘, yet ” !q ,E.

,‘,’

‘,.

.’ ,,

;

,’

,‘,‘I

______,._.“_._.__ --_-_.-_--_-.-._... __.__~.._~_._____,_.._...___ M. W* ‘Sttbttttit pl No. of Tewp~r--__.._ -._.____ iSOmre, No. M. W, crrzyttrc5, (“C) locntiotl ___._ --.--.--_..---..._ ----.-~--_.-.--_-~_--._-._._..._._~_~-_._.,.-__ _..L .erythrocytc 85000 ,5,4,5.8*, 6.3 6 11.g.

Roja clavata Rq/a ttlotrruglti

hen

0votr~~sfcrrin277

Pnktoyl CoA synthckw27g P~tinlbuniins2eo

ox

Nudcotido pbosphotrdnsfcmsc”~ Orniihinckninbtransfcrasc2T* Ornlthipetrn~iscnrbnmyln’sea15 Omithinc trnnscnrbnmylnsc~~6

E coli rat human

Nucleosidcdiphosphokinnsd’~* human

-----I--“--‘--.__

-..-----_..--..--L--..-: Prbtcitt

TABLE 2 (cottritw!)

WP

Pyridinonuclcotidodchydrogcn-

Purinc nuclcouidcphosphorylfl9c3’0

tUC3Q9

Prolhrombin30” Protocollugcnproline hydroxyl-

hunlsn

crythrocytc

erythrocytc

embryo

chick

human

blood

ox

Buctcroidt~~ frr/lylophihrs Aspcripilhrsrriscrr

pancreas plnsmn,nmniotic fluid, pituitnry brnin

28000

84000

248000

GO000

27500

plasnlil

guinea pig guinea pig humnn

rat

77500

strum

pig

guinen

ProlnminckinnscJo5 Protcnscso”

82800

pnncrcas

pig

guinea

pancrcns

pig

28000

113000

G,2”,7.45

G.o*, 6.5,7.0,7.5, 7.8

4.4

n&g.

n.BO

j

‘I

_---.- .- .-.--__-. --__. _

2

5

n,g,

neg, n.g# 0

2 1 3 1

n.g.

n.g. n,g, 2

1 4

6.53 5.3, 5.8,7.4,8,2

5-10

i1.g.

5-10 4 3 2

,5-IO

1 2

r-t.

r.t.

20 n,g, n,g, n,g. n.g. 3

n,g,

4 2

8

2 2 2 3 4 1

1

3.Q 6.9,7,5

(64-8.5) 7.5*, 7,8”, 8.1” 6.22,6.37, 656, 6.72 4,6,4.8* 66 3.5,4,4

4,0*, 10.0* 5.2”, 5.P 5.9,6.8* 5.45,5.9,&3 5.5,5.9,6.25,6.35* 4.65

Gh

30000 4025’ 49000, SGOOO 4.1,4.5 68000 6.2 4.6*

s,p.c. 28000

45000 47700

14100 s,p.c.

81000

guincn

12200

26300

ProcnrbonypcptidnscAl7 ProcnrboxypcptidnscB7’ ProgcstcronobindingglobtMO’ Progcstcroncbindingplnsms protcin303 Proclnstasc77 ProIactin”oJ

pancreaticjuice

plnsmn

hcnrt

47000

13800

llooo

humun

humnn

Oscillnioria ttgtirdhii

pi8

Lntimdrr wttivenom fnhwklt6l Aipkistrodw hnlys biornhofll Cl. perfritgcns iR4cilltts circtdans hcnrt pi6

ProcnrboxypcptidascMO*

Phosphol~pnsoCY Phosphamnnnana&g7 Phosphoryhw n2oB Phosphorylnsob2RB GPhycocyaninaP9

PhospholypnsoA196

PhospholypascAapJ

..,

-

humnn UC’

‘.

Sorylt-RNA 3ynthctnsF Seryj t-RNA aynthctaso317 Staphylokinns# Subtilisin310 ,’ ,’ Su~ti!op,eptidw& ;”

Scrinc mdphhyktsc141

‘,

RNA polymcrasciIs’

Pyruv~tckinasc3’$

RV’,

”

Thymidhickinjitio92s

,”

Thymidinckjm&!

: Thramboplw8tiha~0

,5~~erbxido’dismutnsd13

‘~~s\llphatnscD~~~

Sulpllnta5c

Suiphrit&AaaZo

,,

hog

human

monkcj nionkcy mouse

OX

ox

OX

human ox

Pig’

,’

l?YeMllmolm,~ ncru~irrosu

E, coli S. amw

chicken E. coli

human

rut. oyster oyster guincnpig Ribonucl&dT Ribosr 5-phosphntcisomerns~~~+ Pen

ribosyl Cian8fcrasc3*o Pyrti&z kinad’* / .,

‘) /., : &ii&c thi&nafi&g ‘.

,.

-

?MI’: Pyrophwiphw phospho-

---~~.“-.-..‘_...--_~~-.

Source

wrl/or

M* w.

,_.___._-___-

69500

85000 75000 86000 69OUO 86000

400000 107000 25000 73000

78000

125000 103000 100000

500000

13500

’ 68000

___

liver (&so.) liver liver liver serum kidncy,(cytoJ kidney (mitoch.) ,’ LMcclls(cytoJ LM wlls (mitoch.) IlcLa cc119 (cyto,) I-IcLarclls (mitoch.) thyroid gland

heart

liver str. B str. K12

muscle mantle adduclor muscle pancreas Ic;lf(chloro.) leaf (cyto.) He&acells

.erythrocytc liver

srrbcelldar locnlioti

Orpw

_..__ _____......_._... _.....- .-._-.-.----.---__.-

2’

2 2

,’

--I.--- .--.... - ---.-. PI

5,6,8,4,9.7” 4.5”

9.6

”

7 5.8,5,9,6.0,6.12”,

/;

,’ ”

.’

3 3-4

1

., 22

‘4

4,

,e

n,g, n.g.

‘.

,,,;,

,.,

“, ,@

” ,’ ,(‘() ,:

.’ r _i

Tetnp~r~:, : : ; nmrc ‘, etrzytueS (Oi=,, ‘,,_;I, 8

ISO-

No. oj?

-TL”_._LC----

(U-7.5) 6.0*,‘6.5”: sso”, 5.75’, 6.0, 6875 6.75 6.35* 5.6,6:5’ s.p.c, 8.7,8,8 ” 4,95’ 4.75” 22OOOM), 4.75 1400000, 35000, (25000), .I ,(170000) 6.0 I 53000 6.15.. I 50000 3.9 6.5 .8.4” : 4

Stkrrrit ,__. ..__.~___ No. M. W.

.___.--.......--_.

:.

OX

human

‘Thyrotropin(~SH)3zn~32p

Thyroxine bindingglobulin330

E@crm gracills

groundnut guincripig

Trioscphosphntcisomcrnscle*

Trypsinand chymotrypsin inhibitor337 Trypsinogcn77 Tryptophnnylt-RNA synth&

-.--.-.--I

_-.-.

_.__._ .- -_--

485000 50000 59300

74000 120000 75000

.---.

4

2 2

2

2

.

4.44,G.0”

S.3*,S.8,G,G 4.88 5.0 3,3,3,7*,3,9 3.9*,4.5” 3.62,4.30* 4.1,4.6,7

6.2 5.2 4.G

8.5 8.7*,>9.3

3 I 1 3 2 2 3

1 1

3

1 2

I 1

1

5 3

1 1 1 3

1. 1 2

a

4

4

n,g,

iii&

25

IL&

‘.

2 4 _.__.__ __-- ._-- _. .-. ..-_._--

7,2 8,4 6.25,6.45 G.0 5.5 5.0 5.5, W”, 6.4 5.8,6,2,7.0*, 7.7, 8.0 4.75” 4.8 4.8 4.45

;:2-5.2) 4,3*,4.4*, 4.6”

__._-___ __ - __.__

s,p.c.

120000

37000 58000 s,p,c.

24500

S,pX,

2GSOD

s,p.c. s,p.c,

15000

8.17,8,38”,8.51”, a,70 8,28,8.58*,8.68:

M

‘fc3,

E

‘I

<”

* Tho PI value of the major component. When scvcnor more isozymcsare givenfor ~1singleentry, tho rnngcof pl is givenin parcnthescs,f~l/crwcd by the pl vnhlcsof only the major component(s).Thus. in tbc cnscof tnmino acid oxidnse,whichis rcsolvcdinto 18isozymcs,the vnlucs(5.2-8.4)rgprqscnt the pI rnngc of the 18components, while the values5.60,55.71imd 5,87rcprcscnt the pl vnlucsof the three mnjor components.

~_.__. -. ___._. .._.-__-_-

amnioticfluid

liver

plnccntn str. Vm4

7500

58000 58000

leaf (chloro.) lcuf (cyto.) cytoplnsm chloroplnst piincrcas

56000 53000

28Oo!I 28000 36000

32000

6erum ticrum serum serum crythrocytc muscle

strum

pituitnry

pituitury

St. sa/r~rrinolerrrrn,r Pf.wrcsNIIIloSl~s Cfwysosporhrn~ ligwrrnl - . - .___ -.-.-_

tn~C3sa.33u E coli B TryptopLnyl t-RNA synthctnsoJ’IO human hcillrrs brcvis Tyrosinc a&nmino mutasc3” L-Tyrosincmethylcstcr sulphorrlt trnnsfcrmc341 jnck bcnn Urcnsc313 UDP-glucosyltransfcrnsc3’” pnrslcy humnn VitaminI&,-bindingprotcinJ45 As~wgillrrs Itiger Xylannscn2

Pen

Trioscphosphnteisomcrnsc336

S, awelts a-Toxin Aa3’ S. (lureus u-ToxinB33’ Trnnscobahtmin11331 humnn rnbbit Trnnsfcrrin(npo)33s Trnnsferrin(1 I%*+)333 rnbbit Trnnsfcrrin(2 Fc*+)~” r&bit human Trioscphosphntcisomcrasc334 Trioscphosphnteisonlcrnsc334e335rabbit

senWllrllC

Thyroid stimulatinghormone (TSH’7”’

22

P_ G. RIGHE-ITI,

T. CARAVAGGIO

covering the pH range of interest. Ideally, these pH markers should be coloured proteins or dyes. fn the case of protein markers, they should not be heterogeneous, or at least have a major, easily identificable, band in order to avoid confusion in pH assessments. Studies on the use of pH markers have been reported by ConwqJacobs and Lewin=, Nakbleb et al. 26, Bours’O and Radol$‘. We have listed the&ost coriunon protein and dye markers in Table 1. This table will be followed by.: tf;e .__ com@&ion of data on pI and M.W. values of proteins. En these tables, the most accessible references are given for each entry;. they do not necessarily indicate the source most deserving of credit for the macromolecular parameters given. Some references might have been overlooked. We would appreciaEe comments from other laboratories on missing references and data or on possible errors in these tables. We hope that this compilation wiIi prove useful for teaching and research purposes. 2. ACKNOWLEDGEMENT

This project was supported by resexch grants CT74.00255.04 and No. 75. 00686.115.4756 from Consiglio Nazionale delle Ricerche (C-N-R.), Italy. 3. SUMMARY

Proteins with known isoelectric points ‘@Z), as determined by isoelectric focusing, have been tabuIated. When availabie, the native moIecuIar weight as well as subunit molecular weight and stoichiometry have been reported. For each entry, the source and, when applicable, the organ of origin and/or subcelfular location are given. The pZ values are listed together wit& the respective temperature of pH measurement. Moreover, in the case of proteins displaying microheterogeneity, the major components have been indicated. The table lists a total of approximately 800 pZ values. REFERENCES 1 2 3 4 5 6 7 8 9 10 I1 12 13

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24 76 77 78 79 80 81 82 83 84 85 86 87 X8 59 90 91 92 93 94 95 96 97 98 99 100 101 102 103 104 105 106 107 103 109 110 111 112 113 114 115 116 117 118 119 120 121 122 123 124 125 126 127 128 129 I30 131 132

P. .G. REGHETTX,

T. C~VL4&GIO

T. G. Sanders and W. J. Rutter, Bi~ckernis~?y, 11 (1972) 130. G. k Scheele, f. B&L Ckem., 2.50 (1975) 5375. F. Rob& M. A. Hutchinson and W. L. Beher, J. Biol. Ckem., 246 (1971) 6908. H. Zalkin and L. H. Hwang, 3. Bioi. Ckem., 246 (1971) 6899. P. M. Toorn, T. N. Sohe and A. T. Tu, J. Biol. Ckem., 245 (1970) 2549. E. Ah&en, I(. E. Eriksson and 0. Vesrerherg, Acfa Ckem. SCQIZ~, 2s (1967) 937. E. Ahlgren and K E. Eriksson, Acra Ckem. &and.., 21 (1967) 1193. H. B. Bosman, Biockim. Biophys. Acra, 276 (1972) 180. G. Delisle and F. H. Milazzo, BIbckim. Biophys. Acru, 212 (1970) 503. A. Goldstone and H. Koningg Biockem. J., 141 (1974) 527. A. B. Roy, Biockim. Biophys. Acta, 227 (1971) 129. X R Sahman and A. R. Wihiamson, B&kern. J., 122 (1971) 93. K. A. Cammack, D. I. Marlborough and D. S. Miller, Biuckem. J., 126 (1972) 361. H. K. Robinson, AnaL Biockem.. 49 (1972) 353. B. H. Frank, A. H. Pekar, A. J. Veros and P. P. K. Ho, J_ Biol. Ckem., 24.5 (1970) 37?6. H. Cedar and J. H. Schwartz, J. BiX Ckem., 244 (1969) 4112. G. M&no, M. DeRoss V. Buonocore and V. Scardi, FEBS L&r_, 5 (1969) 347. M. Mutinez-0rr~on, C. TUIZUIO,E_ Chncon% F_ Bossa, A_ Giartosio. F_ Riva and P. Faseha, J. Bioi. Ckem., 242 (1967) 2397. M. Campos-Carrieres and E. A. Mum!, Biockem. f., 135 (1973) 683. M. J. Holland and E. W. Westhead, Biockemiistry, 12 (1973) 2276. F. Falcoz-Kehey, J. Janin, J. C. !&ari, M. Veron, P. Truffa-Bachi and G. N. Cohen, Eur. J. Biockem., 2% (1972) 507. R. R. Fall and P. R Vageios, J. Biol. Ckem., 247 (1972) 8005. W. Berndt, II. HofImann and K, Mueller-Wieiand, 2. Gastroemerol., 6 (1968) 185. J. B. Carlsen and 0. Svensrnark, Biockim. Biopkys. AC~Q,207 (1970) 477. J. R. Maynard and J_ E. Coieman, J. Bio!. Ckem., 246 (1971) 4455 S. Funakoshi and H. F. Deutsch, J. Btoi. Ckem., 244 (1969) 3438. M. J. Carter and D. S. Parsons, Biockim. Bfopkys. Acra, 206 (1970) 190. R. B. Ashworth and T. E. Spencer, Arch. Biockem. Blophys., 142 (1971) 12.2. M. Jonsson and E. Pettersson, Acta Ckem. &and., 22 (1968) 712. A. Ljungquist and IC. B. Augustinsson, Eirr. J. Biockem., 23 (1971) 303. R. Arndt, E. Heymann, \V_ Junge, K. Krisch and H. Hollandt, Eur. .I. Biockem., 36 (1973) 120. D. Wynne and Y. Shahtin, Arch. Biockem. BIbptvs.., 154 (1973) 199. J. L. McCullough, B. A. Chabner and J. R. Bertino, L Biol. Ckem., 246 (1971) 7207. H. L. White and J. C. Wu, Comp. Biockem. PkysioC., 4SB (1974) 575. R. Feinstein and C. Peraino, Biockim. Biopkys. Acra, 214 (1970) 230. P. Coggon, G. A. Moss and G. W_ Sanderson, Pkyrockemisfry, 12 (1973) 1947. A. J. Barret, Biockem. J., 131 (1973) 809. I(. E. Eriksson and W. Rzedowski, Arch. Biockem. Biopkys., 129 (1969) 683. T. M. Wood and S. I. McCrae, Biockem. J., 128 (1972) 1183. C. A. Mapes, C. H. Sue!ter and C. C. Sweely, J. Bioi. Ckem., 248 (1973) 2471. R. J. Carrico and I-Z. F. Deutsch, .i. Biol_ Ckem.. 244 (1969) 6087. A. W. Bemheimer, P. Grushoff and L. S. Avigad, J. Bacrefkd, 95 (1968) 2439. D. MPth&orenssen and F. Fonnum, Biucketm. J., 127 (1972) 229. U. Bradbeck, R. Gentiaetta and S, J. Lundin, Acia Ckem. Sund., 27 (1973) 561. N. Ui, Biockim. Bfopkys. Acta, 229 (1971) 582. G. W. Schwert and S. Kaufman, X Bioi. Ckem., 190 (1951) 807. S. Arvidson ad T. Wadstrijm, 3t.ockz.m. Eiopkys_ A&a, 310 (1973) 418. D. Bobb, Ann. N.Y. Acad. Sci., 209 (1973) 22.5. J. Wilcox, K. Rraut, T. Wade and H. Neurath, Biockinz Biophys. Acta, 24 (1957) 72. P. W. Hochachka and J. K. Lewis, J. Biol. Ckem., 245 (1970) 6567. W. M. Mitcheeil, Biockim. Biopkys. Acra, 178 (1969) 194. A. Gladhaug and H. Prydz, Biocirinz. Biopkys. A&a, 215 (1970) 105. R. G&beck, K. Visti and U. Hakan Stemnan, Biockfm. Bfopkys. Ac;Q, 263 (1972) 721.. U. H&an Stemnan and R. GrSsbeck, Bfockim. Bbpkys_ Acre, 286 (1972) 243. H. R. Herschman and D. R. Hehnski, .l. Biul. Ckem.. 242 (1967) 5360. C. Erlanson and B. Borgstem, Biockim. Biopkys..Acra, 271 (1972) 400. G. Entlicher, J. V. Kostir and J. Kocourek, Bicckim. Btipkys. Acta, 236 (1971) 795.

ISOELECTRIC

POINTS

AND

MOLECULAR

WEIGHTS

OF PRGTELNS

25

133 M. 0. j_ Olson and I. E. Liener, Biochezzzi~rz-y,6 (1967) 3801. 134 P. M. Bayley and A. R. Thomson, Biochem. J., IO4 (1967) 33~. 135 J. Hors& R A Hendon 2nd H. FraenkeEConmt, Biochem. Biophys. Res. Cuzzzmzm., 46 (1972) H. Btoemendal and P. Herbrink, Opfzfld. Res., 6 (1974) 8L J. Bours, Eqz. Eye Res., 16 (1973) 501. 3. Bours, J. Chrunzarogr~, 60 (1971) 225. L. J. Chen and D. A. W&h, Biuchemi~rry, 10 (1971) 3614. B. P. Lin and 3. E. Vamer, Biochim. Biophys. Acfa, 276 (1972) 454. A. E. Braunstein, E V. Goryzchenkova, E. A. Tolosa znd 1. H. Willhardt, &o&m. Bi@zyvs. AC&?, 242 (1971) 247. 142 S. Kashiwarn&a. Y. Ko’&e and D. M. GreeDburg, Biochinr. Biophys_ Acfc, 212 (1970) 501. 143 Y. Okadz and K. Okunuki, J. Biochem. (Tokyo), 67 (1970) 487. 144 L. Spatz uld P. Strittmatter, J. Biol. Clrem., 24g (1973) 793. 145 A. Heaaey uld D. L. WeUer, J. Chenz. E&c_, 47 (1970) 724. 146 T. Flatmark and 0. Vesterberg, Acra Chezzz. .Scarz., 20 (1966) 497. 147 S. N. Vinogradov, K. G. Bitar and K. W. Junk, Biochim. Biophys. Acfa, 257 (1972) 273. 148 G. D. Clark-Wzlker and J. Lascelles, Arch. Biuchem. Biophys., 136 (1970) 153_ 149 W. H. Campbell, W. H. Orme-Johnson and R. H. Burris, Biochem. J., 135 (1973) 617. I50 K. Dus, M. Katagiri, C. A. Yu, D. L. Erbes and I. C. Gunsalus, Biochem. Biophys. Res. Comzzzun., 40 (1970) 423. 151 N. ElIfolk and R. Soininen, Acfa Cizenz. Scmzd, 24 (1970) 2126. 152 B. Goodchild uld J_ N. Smith, Biochn. L-, 117 (1970) 1005. 153 M. L. Dinamarca, L. Levenbook and E_ Valdes, Arch. Biuchenz. Biophys.. 147 (1971) 374. 154 T. Wxlstmm, B&him. Biophys. Acfa, 147 (i967) 441. 155 N. Hiraoka, I. Fukumoto and D. Tsuru, J. Biuchenz. (Tokyo}. 71 (1972) 57. 156 J. C. Janson, Ph. D. Thesis, University of Up@& Uppsala, Sweden, 1972. 157 W. M. Mitchell and J. H. Hash, J. Bioi. Chetzz., 244 (1969) 17. 158 0. Hettand, K. Bryn and F. C. Stormer, Eur. J. Biochem., 21 (1971) 206. 159 L. H. Cohen, P. E. Penner and L. A. Loeb, Azzzz.1V.Y. Acad. Sci., 209 (1973) 354. 160 M. Anai, H. H&aguchi and Y. Takagi, J. Biol. Chem., 247 (1972) 193. 161 S. M. Hadi, D. Kirtik~ and D. A. Goldthwait, Biochemisfry, 12 (1973) 2747. 162 H. Nakayarr, S. Ok&o 2nd Y. ‘Fakagi, Biodzim. Biophys. Acta, 228 (1971) 67. 163 K. G. Mann, F. J. CateIlino and P. A. Hargrave, Biuchemisfry, 9 (1970) 4002. 164 E. I. Scharttz, W. G. Roessler, M. J. Woodbum, J. M. Lynch, H. M. Jacoby, S. M. Silverman J. C. German .md L. Spero, Biochemisfry, 11 (1972) 360. 165 P. C. Cbang 2nd N. Dickie, Biochzizz. Btophys. Acfa, 236 (1971) 367. 166 J. F. Metzger, A. D. Johmson and ?V_ S. Collins, Biochim. Biophys_ Acfa, 257 (1972) 183. 167 J. P. Arbuthnott, B. Billcliffe and W. D. Thompson, FEBS Leff., 46 (1974) 92. 168 N. Tamiya and H. Abe, Bi’uclrenz.J., 130 (1972) 547. 169 T. H. Weber, H. Am arzd C. T. Nordman, Biochim. Biophys. Acfa, 263 (1972) 94. 170 M. R. Rossi-FaneIli, E. Chiancone, P. Vecchini and E. Antonini, Arch. Biochezzz. Biophys., 141 (1970) 278. 171 S. Hartz and H. F. Deutsch, J. Bid. Chem., 244 (1969) 4565. 152 I. Uimshizaki, Y. Niitsu, K. Isbitarti. M. Matsuda and M. Fukuda, Biocirinz. Biaphyr. Acfa, 243 (1971) 187. 173 R. R. Crichton, New Ezgl~ndJ_ Med., 284 (1971) 1413. 174 E_ Alpert. R L. Coston and J. W. Drysdale, Narure (iondon), 242 (1973) 194. 175 B. K. varz E&eel, H. G. ~2x1 Eijk ad B. Leijnse, Acza AYQ~ISZQ~OL, 47 (1972) 59. 176 I. Urushiraki, K. Ishitani and Y. Niitsu, Biuchizzz.Biophys. Acfa, 328 (1973) 95. 177 E. Alpert, J. W. Dry&e and K. J. Isselbacher, Azx_ IV-Y. Acad Sci., 209 (1973) 387. 178 S. Krantr, M. Lober and H. Fiedler, FEBS Left., 11 (1970) 100. 179 H. Kercret and I_ DuvaL Biochemk 57 (1975) 85. 180 J. P. Olson and R. R. Marquardt, kochzkz. kbp/zys. Acfa, 268 (1972) 453. 181 P. W. Ho&.&&a. Biochem. J.. 127 I19721 781. 182 Y. MO, B. G. H&s 2nd R. W. G&y, krch. Biochem. Biophys., 157 (1973) 580. 183 P. E. Penner and L. H. Cohen, .f. Bill. Chem., 246 (1971) 4261. 184 Y. C. Lx md Y. Wacek, Arch. B&hem. Biopkys., 138 (1970) 264. 185 H. N. Johnson and A. G. DeBusk, AP&. BioctIezzz.Ezbpkys:, 138 (1970) 412. 136 137 138 139 140 141

26

‘.

i?:G.RIGHl%T-Q

T. CARAVAGGEO

186 A. E. Moore and B. A. Stone, Biochim. Biophys. ;icta, 258 (1972) &3. 187 R..Chillas, K. M. Doering, G. F. Domagk and M. Rippa, &cit. Biocizent. 5t@kys., 15d (1973) 235. i88 V. M. Der Katoustian, S. H. Idriss-Daouk, R T. HdlaI and Z. L. Awdeh, Biockem. Gettet., 12 (i974) 51. 189 H. E. Abrahams and -J?. Robinson, Biockem. I., 111 (1969) 749. 190 G. Legler, M. van R@off and M. KempBe, Biochim. Biophys. Acta, 257 (1972) 40. 191 J. R. Vase, Phyfockemistry, 11 (1972) 1649. 192 A. SutXer, K. Ortmann and H. Griibach, Biockim. Biopkys. dcta, 258 (1972) 71. 193 K. Ohtsuka and M. Wakabayashi, Enzymologia, 39 (1970) 109. 194 R. Scadurra, C. Cannelia and R Elii, Sci. Too/s, 16 (1969) 17. 195 H. A. Campbell and L. T. IMashbum, Biuchemistry, 8 (1969) 3768. 196 5. Roberts, J. S. Holccnberg and W. C. Dolowy, J. BrX Ckem., 247 (1972) 84.

197 M. Orlowski, P. G. Richman and A. Meister, Biochemisrry,8 (1969) lU48. 198 T. A. Fjelisted, R C. Allen, 8. K. Duncan and W. B. Jakoby, J. Biol. Chem., 248 (1973) 3702. 199 8. GilLham, Biockem. L, 135 (1973) 797. 2GtIR. Jaenicke, D. Schimd and S. Knof, Biockemisfry, 7 (1968) 919. 201 C. M. Smith and S. F. Velick, J. Bioi. Chem., 247 (1972) 273. 292 H. Nagano, T_ Shimada and R Shukuya, J_ Biol. Ckem., 248 (1973) 3052. 203 A. G. Clark, J. N. Smith and T. W. Speiz, Biorhem J., 135 (1973) 385. 2&%R. L. Miller, G. .4. Rzmsey, T. A. Krenitsky and G. B. EIion, Biochemistry, 11 (1972) 4723_ 205 S. H. Grossman and B. Axelrod, J. Biol. Ckem., 248 (1973) 48& 206 J. W. Drysdale, P. G. Righetti and H. F. Bunn, Biockim. Biopkys_ Acta, 229 (1971) 42. 207 G. Braunitzer, K. Hilse, V. RudloE and N. Hilschmann, A&on. Protein Ckem., 19 (1964) 1. 208 M. Per&la, D. Bresciani,G. Guglielmo, V. Russo, F. Rossi, L. Rossi-Bernardi,P. G. Righetti and J. V. Kilmartin, Progr_ Ciin. BioL Res., 1 (1975) 329. 209 H. J. Suderman, C. Yeh-Ku and K. Rondd, Comp. Biockem. Pkysioi., 458 (1973) 515. 210 T. Wads&m, Biockim. Eiophys. Acta, 168 (1968) 223. 211 R. Mallby and T. Wadstrijm, Prot. Biol. Fluids, 17 (1970) 465. 212 T. Y~shida, Biockim. Biopkys. Actu, 71 (1963) 544. 223 R. E. Ferrell and G. B. Kitto, Biochemistry, 9 (1970) 3053. 214 B. Wurster and B. Hess, Eur. b. Biochem., 36 (1973) 68. 215 J. R. Pringle, Biockem. Biopkyx Res. Commcm.. 39 (1970) 46. 216 0. Vesterberg, Biochim Biopkys. Acta. 168 (1968) 218. 217 0. Vesterberg,T. Wadstriim, K. Vesterberg,H. Svensson and B. Malmgren, Biochim. Bigpkys. Acta, 133 (1967) 435. 218 B. E. Noyes and R. A. Bradshaw, J. Biol. Ckem., 2$8 (1973) 3052. 219 B. E. Noyes, B. E. Ghtthaar, J. S. Garavelli and R. A. Bradshaw, Proc. Nat. Acad. Sci. Lr.S.. 71 (1974) 1334. 220 W, J. Arnold and W. N. Kelley, J_ Bioi. Gem., 246 (1971) 7398. 221 D. F. Waugh, Advan. Protein Chem., 9 (1954) 325. 222 0. Vcsterberg and B. Berggren, Ark. Kemi, 27 (1966) 119. 223 Z. D. Meachum. Jr., H. J. Calvin, Jr. and H. D. Braymer, Biochemistry, LO (1971) 326. 224 J. A. Ill&worth, Biochem. L, 129 (1972) 1119. 225 D. L. Weller, A. Heaney and R. E. Sjogren, Bioishim. Bio_chys. Acta, 168 (1968) 576. 226 R. H. Amxnerstedt,H. Miihter, K. A. Decker and W. A. Wood, L Biol. Ckem., 246 (1971) 2069. 227 H. Yamasaki aud T. Moriyama, Biockim. Biopkys. Acta, 242 (1971) 637. 228 M. Jousson. E. Petterssonaild 3. Reinhvnmar Acta Chem. Scud., 22 (1968) 2135. 229 H. Mosbach, Biochim. Biopkys. Acta, 73 (1963)‘204. 230 W. Schaeg, R. Sing51 and H. BIobel, Biochim. Biophyys. Acta, 268 (1972) 542. 231 J. Peciersen,f. Phys_ Ckem., 51 (1947) 164. 232 S. S&leg&-Haneter, P. Hore, K. R. Kerry and G; Semen- Biockim. Biophy. Acta, 258 (1972) 506. 233 E. Kolh and I. I. Harris, Bhchem_

J_, 1X.(1971) 76~: 234 -R ‘Fawxzendand S_ N. Tiieff, L Amer. Fizz_ Sot, 79 (2957) 3613. 235 S. Fre&iksscb, Anal. Biockem., 50 (1972) 575. 236 A. Carlsttim and 0. Ve&rbefg, Acta Chem. Scmrd, 21 (1967) 2%. 237 W. J. Broughton, M. J. Diiworth and C. A. Godfrey, Stiuiem. L, 127 (1972) 309. 233 V. R-en, I%. H: Weber z.nd R. GrZsbeck, Eiu. X B&b&em.., 38 (1973) 193.

ISOELECTRJC

239 240 24! 242 243 244 245 246 247 248 249 250 251

252 253 254

255 256 257 258

POINTS

AND

MOLECULAR

WEIGHTS

OF PROTEINS

27

I. G. Chirikjian, K. Kanagahngarn, E. Lau and J. R. Fresco, J. Brbc Chem., 248 (1973) 1074. G. S. Has&g, Bkxkim. Biopizys. Acra, 242 (1971) 381. M. L. Cohn and L R McManus, Bi’chim. Biophys. Acta, 276 (1972) 70. N. Catsirnpoolas,Arch. Biochem. Bioph~s., 131 (1969) 185. F. C. Stevens, D. M. Brown and L. E. Smith, Arch. B~oc/zem_ Bibphyys., 136 (1970) 413. J. P. Christopher, E K. Pistorius and B. Axelrod, Biochim. Biopkys. Acta, 284 (1972) 54. C. E. Eriksson and S. G. Svensson, Biochim. Biophys. Acta, 198 (1970) 449. S. Fredriksson, AnoC. Biochem., 57 (1974) 452. 3. E. W&son, Arck. Biackem. Biopkyq l&I (1971) 216. J. L. Denburg and W. D. McElroy, Biochemistry, 9 (1970) 4619. H. Kercret and 3. Duvd, Biuchemie, 57 (f97.5) 85. D. N. Ward, L. E. Reichart, Jr., B. A. Fitak, H. S. Nahm, C. M. Sweeney and J. D. Neill. Btochemisfry, 10 (1971) 1796. K. Haino, B~ochlm. Biopkys. Acta, 229 (1971) 459. G. Lundbiad, 0. Vesterberg, R. Zimmerman and J. Lind, Acta Chem. Scar& 26 (1972) 1711. D. W. Fodge, R. W. Gracy and B. G. Harris, Bfochim. Biophys. Acta, 263 (1972) 271. F. E. Ruth and P. R. Vagefos, J. Blof. Ckem., 248 (1973) 8086. M. Saitz, T. &en&a uld Y. Matsushima, J. Biuchem. (Tokyo), 70 (1971) 827. A. P_ Surguchev, I. 6. Surgucheva, T. M. Errnokhima and G. N. Zaitseva, Biochim. Biophys. Acza, 224 (1970) 623. H. Delin&e and B. J. Radola, Biochim. Biophys. Acfa, 214 (1970) 178. E. B&a, J. K. Dorsey, J. Marr, W. W. Cleland and J. W. Porter, J. Bid. Chem., 245 (1970)

5450. 259 A. H. A. van den Oord, J. J. Wesdorp, A. F. van Darn and J. A. Verheij, Fur_ J. Giochem., (1969) 140. 260 T_ D. Poliard and E. D. Kern, J. Biol. Chum., 245 (1973) 4652. 261 B. Lonnerdai and J. Ch. Janson, Biockhim. Biopkys. Acra, 278 (1972) 175. 262 T. Horio, R. G. Bartsch, T. Kakuno and M. D. Karen, f. Biol. Chem., 2441(1969) 5899. 263 T. W. Moon and P. W. Hochachka, Biochem. J., 123 (1971) 695. 264 V. Bcxchini, Biockim. Biophys. Acfa, 243 (1971) 420. 265 R. H. Ange!etti and R. A. Bradsbaw, Proc. Nat. Acad Sci. U.S., 65 (1971) 2417. 266 A. R. Neuratb, R. W. Hartzell and B. A. Rubin, Erperientziz, 26 (1970) 1210. 267 A. P. Kendal, M. P. Kiley and E. A. Eckert, Biochim. Biophys. Acta, 317 (1973j-28_ 268 W. L. St&l and R. D. OToolz, Biachim. Biopkqs. Acta, 268 (1972) 480. 269 P. Davies, G. A. Rita, K. Krakauer and G. Weissman, Biochem. f., 123 (1971) 559. 270 B. k Notton, E. J. Hewitt and A. H. Fielding, Phytochemistry, 11 (1972) 2447. 271 R. R. Eady, B. E. Smith, K. A. Cook and J. R. Postgate, Biochem. J., 128 (1972) 655. 272 Y. C. aeng, R. P. Agarwd and R. E. Parks, Jr., Biochemistry, 10 (1971) 2139. 273 E. F. Brunngraber and E. Cbargaf?, Biochemisrry, 12 (1973) 3005. 274 C. Peraino, L. G. Bunville and T. N. Tahmisian, J. Biai. Chem., 244 (19693 2241. 275 S. Arashima and I. Matsuda, Biochem. Bioplgvs Res. Common., 45 [1971) 145. 276 M. Marshal1 and P. P. Cohen, J. Bioi. Chem., 247 (1972) 1641. 277 R. V. Wenn and J. Wifhatns, Biuchem. J_, 105 (1968) 69. 278 B. Middleton, Biuchem. J., 132 (1973) 717. 279 J. Bar-Tana and G. Rose, B&hem. J., 131 (1973) 443. 280 C. Gerday and J. C. Tewis, Biochfm Biophys. Acta, 271 (1972) 320. 281 0. Vesterberg, Acta Chem. Scan& 27 (1973) 2415. 282 R. C. Williarnls, Jr. and T. G. Rajagopalan, J. Bfol. Chem., 241 (1966) 4951. 283 K_ G. Paul and T. Stigbrand, Acta Chem. Stand, 24 (1970) 3607. 284 H. Delino% and B. I. Rado!a, B&him. Biophys. Acta, 200 (1970) 404. 285 A. Cecil and J. Ogston, Biochem. J., 49 (1951) 105. 286 A. Femandez-Sbrensenand D. M. Carlson, J. Biol. Ckem., 246 (1971) 34%. 287 B. Lerch and G. Wolf, Biochim. Biophys. Acta, 258 (1972) 206. 288 T. E. Srnithh.Arch. B&hem. Biophys_.. 128 (1968) 611. 289 T. E. Smith, f. BioL Gem., 246 (1971) 4234. 290 S. Harshman and H. R. Six, Biochemistry, 8 (1969) 3423. 291 W. A. Scott and T. Abramsky, J. BioL Ckem., 245 (1973) 3535. 292 K. K. Tsuboi and K. Fukunaga, J. Bid. Chem., 246 (1971) 7586.

10

28

P. G. RIGHEITI,

T. CARAVAGGIO

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