inhibition of dehydrogenases by snake venom
- 31 March 1939
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 33 (4), 407-411
- https://doi.org/10.1042/bj0330407
Abstract
In continuation of previous studies on the inhibitory effect of snake venoms on glycolysis and fermentation (Quart. J. exp. Physiol. 26, 299; 27, 50; 27, 375) the effect of black tiger snake venom (Notechis scutatus) on the following dehydrogenases and oxidases was tried: lactic, malic, [beta]-hydroxybutyric, amino acid, [alpha]-glycerophosphate, succinic dehydrogenases; cytochrome, xanthine, uric acid oxidases. The venom inactivated in small concs. those dehydrogenase systems the action of which was dependent on the presence of a coenzyme of nucleotide nature. The inactivation was due to a destruction of the coenzymes by the venom. The destruction was an enzymatic process caused by the action of a nucleotidase which was present in many venoms. The nucleotidase acted on coenzyme I (pyridine-di-phos-phonucleotide) by hydrolysing the pyrophosphate linkage in the molecule. In view of the fact that the metabolism of the brain was mainly a carbohydrate metabolism which was especially dependent on the presence of coenzyme I, the neurotoxic effect of the venom was probably due to its destructive action on this substance.This publication has 4 references indexed in Scilit:
- Phosphoesterases of bone and snake venomsBiochemical Journal, 1938
- The β-hydroxybutyric dehydrogenase of animal tissuesBiochemical Journal, 1937
- α-Glycerophosphate dehydrogenaseBiochemical Journal, 1936
- The mechanism of the reaction of substrates with molecular oxygen. IBiochemical Journal, 1935