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The in vitro neuromuscular blocking properties of sea snake (Enhydrina schistosa) venom
In addition to the insects, the author discusses other common terrestrial arthropods and devotes sections to prehistoric insects, insect pests, making and storing insect collections, etc. It has bcen many years since 1 have read a book so packed full of information of the insects of a given area . Although one may quibble about soma statement in the text, it is an excellent reference work for any biologist working with arthropods, including the venomous species . F.E.R . WALrcER, M. J. A. and YEOH, P. N. (Department of Pharmacology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia). The in vitro neuromuscular blocking properties of sea snake (Enhydrlna schistosa) venom. F.rlr . J. Pharmac. 28, 199, (1974) . THE NEUROMUSCULAR blocking properties of a sea snake (Bnhydrina schistosa) venom have been compared with those of n-tubocurarine and diallylbisnortoxiferine in seven different muscle preparations from five species. The sensitivity (EO ) of each muscle to acetylcholine and carbamylcholines was also compared . The sensitivity to acetylcholine varied markedly, whilst variation to carbamylcholine was much less, presumably because of differences in the content of acetylcholinesterase in the different tissues . The extraocular muscles of rats and monkeys were the most sensitive to the venom, whereas the toad rectos abdominis and leech muscles were the least. Variations in sensitivity to the venom were much greater than those to n-tubocurarine and diallylbisnortoxiferine. (' .Y .L . CHACxo, G. E., BARNOLA, F. V., Vll.LEGAS, R. and GOLUMAN, D. E. (Dtpartments of Biochemistry and Physiology, Medical College of Pennsylvania, Philadelphia, Pennsylvania, U.S .A . and Centro de Biofisica y Bioquimica, Instituto Venezolano de Investigaciones Cientificas, Caracas, Venezuela) . The bindingof tetrodotoxin to (an) axonal membrane fraction isolated from garfish olfactory nerve. Biochem. biophys. Acta 373, 308 (1974) .
A et.A~tA membrane fraction isolated from homogenized gafish olfactory nerve tissue by sucrose gradient centrifugation has been studied with respect to its equilibrium binding of 'H-labelled tetrodotoxin. Tetra dotoxin binds to the membrane fraction with a dissociation constant of S" 5 x 10 - ° M and a maximal binding of 3"7 pmoles of tetrodotoxin per mg of membrane protein. Based on these data and measured values of the nerve membrane composition, density and thickness, it was determined that the number of tetrodotoxin bindingsites is 6"2 per um' of surface area of membrane. A comparison is made lxtween properties of plasma membrane fractions isolated from garfish olfactory nerve and those of wnesponding fractions obtained from lobster leg nerves. S.L.F . FUFiRMAN, F. A. (Hopkins Marine Station, Pacific Grove, Calif. 94950) . Fish eggs . Toxic Constituents of Animal Foodstuffs, Academic Press, Inc., p. 74 (1974) .
THE roxrcrrr of fish eggs is reviewed, including that of tetrodotoxin from puff and porcupine fish eggs, the lipoproteins from cabezon and blenny rce, and the toxins of certain cyprinid fishes, pikes, and gars. The suspected toxicity of the roe and several other fishes is noted. This is a concise, well-written review on the problem of ichythyo-otoxism . F.E .R . HAUFAr, J., MAVtE, M., SUS4MAN, A. and BARGErZr, J. P. (Department of Biochemistry, University of Geneva, Geneva, Switzerland). The major lethal neurotoxin of the venom of Naja naja philippinensls . Int. J. Peptide Protein Res. 6, 201 (1974) . A rrEUROroxrrr of Naja n. philippinensis venom was purified, mostly by chromatography on different Sephadexes. The final product had an Ln of 005 pg per g mouse (i .v .), a mol. wt of 6867, an IEP of pH 108 and an unusually high molecular O.D . of 14 "300, at 280 nm . Rotation dispersion and circular dichroism favour a B sheet structure. It is a `short toxin', numbering 61 amino acid residues . The residues 1-31 and 50-61 have been sequenced. Interesting is an alanine residue in position 11, similar to alanine in 12 of the short toxins of Dendroaspis viridis, D. polylepis and in 9 of the peptide T III of N. nigricollis mossambica. Most remarkable and till now unique arc two tryptophane residues in the important position 27 and 28 ; T III also has two tryptophane residues, however, in 20 and 29 . TOXICON 1973 Yol. I3
A et.A~tA membrane fraction isolated from homogenized gafish olfactory nerve tissue by sucrose gradient centrifugation has been studied with respect to its equilibrium binding of 'H-labelled tetrodotoxin. Tetra dotoxin binds to the membrane fraction with a dissociation constant of S" 5 x 10 - ° M and a maximal binding of 3"7 pmoles of tetrodotoxin per mg of membrane protein. Based on these data and measured values of the nerve membrane composition, density and thickness, it was determined that the number of tetrodotoxin bindingsites is 6"2 per um' of surface area of membrane. A comparison is made lxtween properties of plasma membrane fractions isolated from garfish olfactory nerve and those of wnesponding fractions obtained from lobster leg nerves. S.L.F . FUFiRMAN, F. A. (Hopkins Marine Station, Pacific Grove, Calif. 94950) . Fish eggs . Toxic Constituents of Animal Foodstuffs, Academic Press, Inc., p. 74 (1974) .
THE roxrcrrr of fish eggs is reviewed, including that of tetrodotoxin from puff and porcupine fish eggs, the lipoproteins from cabezon and blenny rce, and the toxins of certain cyprinid fishes, pikes, and gars. The suspected toxicity of the roe and several other fishes is noted. This is a concise, well-written review on the problem of ichythyo-otoxism . F.E .R . HAUFAr, J., MAVtE, M., SUS4MAN, A. and BARGErZr, J. P. (Department of Biochemistry, University of Geneva, Geneva, Switzerland). The major lethal neurotoxin of the venom of Naja naja philippinensls . Int. J. Peptide Protein Res. 6, 201 (1974) . A rrEUROroxrrr of Naja n. philippinensis venom was purified, mostly by chromatography on different Sephadexes. The final product had an Ln of 005 pg per g mouse (i .v .), a mol. wt of 6867, an IEP of pH 108 and an unusually high molecular O.D . of 14 "300, at 280 nm . Rotation dispersion and circular dichroism favour a B sheet structure. It is a `short toxin', numbering 61 amino acid residues . The residues 1-31 and 50-61 have been sequenced. Interesting is an alanine residue in position 11, similar to alanine in 12 of the short toxins of Dendroaspis viridis, D. polylepis and in 9 of the peptide T III of N. nigricollis mossambica. Most remarkable and till now unique arc two tryptophane residues in the important position 27 and 28 ; T III also has two tryptophane residues, however, in 20 and 29 . TOXICON 1973 Yol. I3