蛇毒の酵素化学的研究(第5報)ヒャッポダ毒より致死活性物質Ac_3-Proteinaseの精製

概要

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Ac_3-Proteinase was purified from the lyophilized venom of Agkistrodon acutus using gel filtration on a Sephadex G-75 column, followed by chromatography on diethylaminoethyl (DEAE)-Sephadex A-50,DEAE-Sephacel and DEAE-Sephacel rechromatography. By these procedures, 22.7 mg of purified preparation was obtained from 1 g of crude venom. The purified preparation was homogeneous as judged by disc electrophoresis over polyacrylamide gel at pH 8.3 and isoelectric focusing. Ac_3-Proteinase possessed both lethal and hemorrhagic activities. These and proteolytic activities were inhibited by ethylenediaminetetraacetic acid (EDTA), cysteine or antiserum, but not by soybean trypsin inhibitor (SBTI), p-chloromercuribenzoate (PCMB) or diisopropyl fluorophosphate (DFP). The molecular weight of Ac_3-proteinase was estimated to be about 57000 by SDS-polyacrylamide gel electrophoresis, and the isoelectric point was found to be pH 4.7,indicating that the protein was acidic. The minimum hemorrhagic dose, LD_<50> and proteolytic activities of the purified preparation were 0.95μg, 108μg/mouse, and 0.253 unit/mg, respectively. Both Ac_1- and Ac_2-proteinases were simple proteins, while Ac_3-proteinase was a glycoprotein.
公益社団法人日本薬学会の論文
1979-12-25