蛇毒の酵素化学的研究(第2報) : ヒャッポダ毒より致死活性物質Ac<SUB>1</SUB>-Proteinaseの精製

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タイトル別名
  • Enzymochemical Studies on Snake Venoms. II. : Purification of Lethal Protein Ac<SUB>1</SUB>-Proteinase in the Venom of Agkistrodon acutus
  • 蛇毒の酵素化学的研究-2-ヒャッポダ毒より致死活性物質Ac1-Proteinaseの精製
  • ダドク ノ コウソ カガクテキ ケンキュウ 2 ヒャッポダ ドク ヨリ チシ
  • Enzymochemical studies on snake venoms-II. Purification ot lethal protein Ac1-Proteinase in the venom of Agkistrodon acutus

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A proteolytic enzyme named Ac1-proteinase was isolated from the venom of Agkistrodon acutus by a combination of gel filtration on Sephadex G-75 and chromatographies on diethylaminoethyl (DEAE)-Sephadex A-50, DE32 cellulose, and DEAE-Sephadex A-50. By these procedures, 38 mg of purified preparation was obtained from 1 g of crude venom. Ac1-proteinase also had lethal and hemorrhagic activities. These three activities were inhibited by ethylenediaminetetraacetic acid (EDTA) or cysteine but not by soy bean trypsin inhibitor (SBTI) or diisopropyl fluorophosphate (DFP). The preparation was homogeneous as judged by disc electrophoresis at pH 8.3, and pH 7.5 polyacrylamide gels, immunodiffusion, and isoelectric focusing. The molecular weight of this protein was determined to be approximately 24500 and the isoelectric point was found to be pH 4.7 by isoelectric focusing with carrier ampholyte. The minimum hemorrhagic dose, LD50 and proteolytic activities of this protein were 0.223 and 76.5μg mouse and 0.544 unit, respectively. This protein did not contain any carbohydrates or nucleic acids.

収録刊行物

  • 薬学雑誌

    薬学雑誌 97 (5), 507-514, 1977

    公益社団法人 日本薬学会

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