STRUCTURE OF SNAKE TOXINS AND THEIR AFFINITY TO ACETYLCHOLINE-RECEPTOR OF FISH ELECTRIC ORGAN

被引：66

作者：

ISHIKAWA, Y ^{[1
]}

MENEZ, A ^{[1
]}

HORI, H ^{[1
]}

YOSHIDA, H ^{[1
]}

TAMIYA, N ^{[1
]}

机构：

[1] TOHOKU UNIV, DEPT CHEM, SENDAI, MIYAGI 980, JAPAN

来源：

TOXICON | 1977年 / 15卷 / 06期

关键词：

D O I：

10.1016/0041-0101(77)90098-8

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The affinity of sea snake [Laticouda semifasciata, Aipysuru laevis] and elapid snake [Burgorus multicinctus] venom components with neurotoxic activity, and their chemically modified derivatives, to the acetylcholine receptor of ray (Torpedo marmorata) electric organ was studied by following the competition in binding with labeled toxin .alpha. Naja nigricollis venom. Some of the unusual toxins, which lack some of the invariant residues among neurotoxins, have lower affinity. A parallel relationship between the affinity and LD50 was observed.

引用

页码：477 / 488

页数：12

共 52 条

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