1969
DOI: 10.1016/0005-2795(69)90262-1
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Characterization of the enzymatic and biological activities of snake venoms by isoelectric focusing

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Cited by 27 publications
(7 citation statements)
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“…On the basis of the data presented in the previous section, it appears that hemorrhagic toxin e is a slightly acidic protein (pi = 5.6) containing no carbohydrates. It is of interest that hemorrhagic fractions isolated from the venom of Agkistrodon rhodostoma (Malayan pitviper) are also slightly acidic, having the pi values of 5.6 and 6.1, respectively (Toom et al, 1969).…”
Section: Discussionmentioning
confidence: 99%
“…On the basis of the data presented in the previous section, it appears that hemorrhagic toxin e is a slightly acidic protein (pi = 5.6) containing no carbohydrates. It is of interest that hemorrhagic fractions isolated from the venom of Agkistrodon rhodostoma (Malayan pitviper) are also slightly acidic, having the pi values of 5.6 and 6.1, respectively (Toom et al, 1969).…”
Section: Discussionmentioning
confidence: 99%
“…1 ,3 -5 Among the tox ins re sponsible for these local effects, hae morrhagic factors w ere isolated from various viperid venoms. 6 Eve n though some of the se haemorrhagic fac tors are devoid of p rote olytic ac tivitie s, [7][8][9][10][11] the y are charac te rise d as me talloproteinases. 6 Some of the se factors digest prote ins from the ex trace llular matrix , and this prop erty has be en related to the pathogeny of haemorrhagic lesions.…”
Section: Introductionmentioning
confidence: 99%
“…It was shown that venoms from sea snakes are much simpler in composition than the venoms of the land snakes, as evidenced from the isoelectric focusing distribution patterns (Toom et al, 1969). Similarly, sea snake venoms contain fewer enzymes than those of land snakes.…”
Section: Enzymesmentioning
confidence: 99%
“…Similarly, sea snake venoms contain fewer enzymes than those of land snakes. Venom of Enhydrina schistosa lacks proteolytic and arginine ester hydrolyzing activity (Toom et al, 1969). Venoms of Laticauda colubrina and Laticauda semifasciata do not hydrolyze p-toluenesulfonyl-L-arginine methyl ester and iV-benzoyl-L-arginine ethyl ester, while these substrates are easily hydrolyzed by venoms of some terrestrial snakes (Tu et al, 1966).…”
Section: Enzymesmentioning
confidence: 99%