蛇毒の酵素化学的研究(第4報)ヒャッポダ毒より致死活性物質Ac_2-Proteinaseの精製

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Ac_2-proteinase, one of proteinases of the venom of Agkistrodon acutus was purified by gel filtration on Sephadex G-75,followed by chromatographies on diethylaminoethyl (DEAE)-Sephadex A-50 and DE52 cellulose. By these procedures, 12.8 mg of purified preparation was obtained from 1g of crude venom. The purified preparation was homogeneous as judged by disc electrophoresis over polyacrylamide gel at pH 8.3 and isoelectric focusing. Ac_2-proteinase also 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 or diisopropyl fluorophosphate. The molecular weight of Ac_2-proteinase was estimated to be about 25000 by SDS-polyacrylamide gel electrophoresis, and the isoelectric point was found to be pH 4.9 by isoelectric focusing with carrier ampholyte. The minimum hemorrhagic dose, LD_<50>, and proteolytic activities of the purified preparation were 0.431μg, 110μg/mouse, and 0.173 unit/mg, respectively. This protein did not contain any carbohydrates or nucleic acids.
公益社団法人日本薬学会の論文
1978-11-25