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<SUB>3</SUB>-Proteinaseの精製

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タイトル別名
  • Enzymochemical Studies on Snake Venoms. V. Purification of Lethal Protein Ac<SUB>3</SUB>-Proteinase in the Venom of Agkistrodon acutus
  • 蛇毒の酵素化学的研究-5-ヒャッポダ毒より致死活性物質Ac3-Proteinaseの精製
  • ダドク ノ コウソ カガクテキ ケンキュウ 5 ヒャッポダ ドク ヨリ チシ

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Ac3-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. Ac3-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 Ac3-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, LD50 and proteolytic activities of the purified preparation were 0.95μg, 108μg/mouse, and 0.253 unit/mg, respectively. Both Ac1- and Ac2-proteinases were simple proteins, while Ac3-proteinase was a glycoprotein.

収録刊行物

  • 薬学雑誌

    薬学雑誌 99 (12), 1161-1167, 1979

    公益社団法人 日本薬学会

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