蛇毒蛋白の研究 (第1報)

Abstract

Isolation of snake venoms by paper microelectrophoresis was carried out on 11 kinds of venomous snakes, Naja naja atra Cantor (I), Naja naja naja (II), Naja hanah (III), Bungarus multicinctus Blyth (IV), Vipera russellii formosensis Maki (V), Trimeresurus mucrosquamatus Cantor (VI), Trimeresurus gramineus stjnegeri Schmidt (VII), Trimeresurus flavoviridis flavoviridis Hallowell (VIII), Trimeresurus okinavensis Boulenger (IX), Agkistrodon acutus Guenther (X), and Agkistrodon halys blomochoffi Boie (XI). It was found that the venom from same species gave similar pattern. The venom from Naja species was composed of two or three bases and that of Agkistrodon species contained a large amount of acid proteins. Each protein on the filter paper from the venom of Formosan cobra (I) was cut out and their enzymatic action was examined. It was found that lecithinase was present in electrically neutral portion while cholinesterase was at pH 6.0, slightly to the cathodic side. Cobra venom purified by fractional precipitation with ammonium sulfate and acetone precipitation was found to be proteose, being about eight times more poisonous than the original venom, but showed no activity of lecithinase, cholinesterase, and l-ophio amino acid oxidase, being electrically almost neutral. The kinds of amino acids constituting the venoms of (I) and (X), which showed completely different electric characteristics, were examined by two-dimentional paper chromatography and paper ionophoresis by which 15 kinds of amino acids, including leucine and alanine, were detected. No difference in the kinds of amino acids constituting these two venoms was found.