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Hydrolysis of alanyl-L-glutamine (ALA GLN) and acetyl-L-glutamine (AC-GLN) in various tissues of rats and of man
P.43
DICARBOXYLIC Rll TACCHIWO, Pepartmn-of
F Warino, Surgery,
ACIDS VERSUS TRADITIONAL I Arcieri:, G Win rone., Depar 9sent of Hedicine
,
LIPIDS IN TPN.
II Caotagnet;, G Gaabassi* Catholic University Rose
Italy
Jy-products of , A-qxidation when as In I-oxidation II airlent, However #onocarboxylic acids oneaoxidable mediur-chain *P. peroxisolialcarni ine independent litochondrialand c toplaslattic evi 4 ence exists of in total parenteral 4 le use as energy substrate B-oxidation. For this reaso",ue su posed their posse (IL) infusion.Along 9 erent response to NCDFA versus Intralipid the dlf nutrition and investigated
Wediua
chain
dicarboxylic
fatty
acids
chosen the C9 acid (azelaic HCDFA we have huaans. The metabolic response to intravenous fasting nale volunteers healthy overni ht P our of then were adainistered, ainutes; to were aetabolic paralteters Respiratory and the infusion for 2bO ainutes. Baseline b0 minutes
(HCDF:)re
;cu,u,;$dered
acid:AA) because of the previous experience of ,use administration of AA versus IL of AA d& an infusion of T gaeva’ua’ed that received 10 ga of with the same aodalit as control, ca Y orlaetry fro@ the beginning . by indirect evaluated 80 ainutes
in
‘\\ IL. of
2bO minutes
P.44 HYDROLYSIS OF ALANYL-L-GLUTAMINE
~ALH GLN) AND ACETYL-L-GLUTAMINE (AC-GLN) IN VARIOUS TISSUES OF RATS AND OF MAN. S. PBssler, A. GrUnfeld, 0. Berthold, M. Neuhzuser-Berthold. Institute of Physiological Chemistry, Johannes Gutenberg-Universitzt, Mainz, FRG.
ALA-GLN and AC-GLN are presently being discussed as glutamine source for parenteral nutrition. In this study hydrolysis capacity of various tissues for ALA-GLN and AC-GLN in rats and in man were compared. Method: Peptidase activity was estimated by applying a ninhydrin assay. Buffered solutlons of ALA-GLN and AC-GLN were added to various tissue homogenates. After incubation for different time intervals the reaction was stopped. Hydrolysis was measured by the increase of extinction due to degradation of GLY-GLN and AC-GLN to the constituent free amino acids. Vmax and Km were calculated from plotting the initial velocity of the reaction against the substrate concentration according to Hofstee. Results:
Vmax: ,umol/min*g tissue
Km: mmol/l
liver kidney muscle lung plasma
ALA-GLN rat man 61 356 615 492 ,6 12 56 89 -02 .2
ALA-GLN man rat 1.7 1.0 11 1:; 1'3 ;, ;:; ,:2
I
AC-GLN rat man 1.3 3.6 4.5 5.2 ___ ___ ___ ___ _____
AC-GLN rat man 10.6 13.4 !0:8 -_-__-_
!_3:_4 ::::
Ccnclusions: The results show that hydrolysis activity is much higher for ALA-GLN than fbr AC-GLN. These data also encourage to transfer results obtained from long-term infusion studies in rats to man.
72
DICARBOXYLIC Rll TACCHIWO, Pepartmn-of
F Warino, Surgery,
ACIDS VERSUS TRADITIONAL I Arcieri:, G Win rone., Depar 9sent of Hedicine
,
LIPIDS IN TPN.
II Caotagnet;, G Gaabassi* Catholic University Rose
Italy
Jy-products of , A-qxidation when as In I-oxidation II airlent, However #onocarboxylic acids oneaoxidable mediur-chain *P. peroxisolialcarni ine independent litochondrialand c toplaslattic evi 4 ence exists of in total parenteral 4 le use as energy substrate B-oxidation. For this reaso",ue su posed their posse (IL) infusion.Along 9 erent response to NCDFA versus Intralipid the dlf nutrition and investigated
Wediua
chain
dicarboxylic
fatty
acids
chosen the C9 acid (azelaic HCDFA we have huaans. The metabolic response to intravenous fasting nale volunteers healthy overni ht P our of then were adainistered, ainutes; to were aetabolic paralteters Respiratory and the infusion for 2bO ainutes. Baseline b0 minutes
(HCDF:)re
;cu,u,;$dered
acid:AA) because of the previous experience of ,use administration of AA versus IL of AA d& an infusion of T gaeva’ua’ed that received 10 ga of with the same aodalit as control, ca Y orlaetry fro@ the beginning . by indirect evaluated 80 ainutes
in
‘\\ IL. of
2bO minutes
P.44 HYDROLYSIS OF ALANYL-L-GLUTAMINE
~ALH GLN) AND ACETYL-L-GLUTAMINE (AC-GLN) IN VARIOUS TISSUES OF RATS AND OF MAN. S. PBssler, A. GrUnfeld, 0. Berthold, M. Neuhzuser-Berthold. Institute of Physiological Chemistry, Johannes Gutenberg-Universitzt, Mainz, FRG.
ALA-GLN and AC-GLN are presently being discussed as glutamine source for parenteral nutrition. In this study hydrolysis capacity of various tissues for ALA-GLN and AC-GLN in rats and in man were compared. Method: Peptidase activity was estimated by applying a ninhydrin assay. Buffered solutlons of ALA-GLN and AC-GLN were added to various tissue homogenates. After incubation for different time intervals the reaction was stopped. Hydrolysis was measured by the increase of extinction due to degradation of GLY-GLN and AC-GLN to the constituent free amino acids. Vmax and Km were calculated from plotting the initial velocity of the reaction against the substrate concentration according to Hofstee. Results:
Vmax: ,umol/min*g tissue
Km: mmol/l
liver kidney muscle lung plasma
ALA-GLN rat man 61 356 615 492 ,6 12 56 89 -02 .2
ALA-GLN man rat 1.7 1.0 11 1:; 1'3 ;, ;:; ,:2
I
AC-GLN rat man 1.3 3.6 4.5 5.2 ___ ___ ___ ___ _____
AC-GLN rat man 10.6 13.4 !0:8 -_-__-_
!_3:_4 ::::
Ccnclusions: The results show that hydrolysis activity is much higher for ALA-GLN than fbr AC-GLN. These data also encourage to transfer results obtained from long-term infusion studies in rats to man.
72