魚類のコラーゲナーゼに関する研究-II

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タイトル別名
  • Studies on collagenase in fish. II. Some properties of a collagenase from the pyloric caeca of Seriola quinqueradiata.
  • 魚類のコラーゲナーゼに関する研究-2-ハマチ幽門垂コラーゲナーゼの性質〔英文〕
  • ギョルイ ノ コラーゲナーゼ ニカンスルケンキュウ 2 ハマチ ユウモンスイ
  • Some Properties of a Collagenase from the Pyloric Caeca of <i>Seriola quinqueradiata</i>

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A collagenolytic enzyme has been isolated from the pyloric caeca of yellow-tail, Seriola quinqueradiata, The pyloric caecum collagenase acts on native collagen fibrils and on collagen in solution. The activity is maximal at pH 8. 5. Diisopropyl fluoro-phosphate, N-tosyl-L-lysylchloromethane, soybean trypsin inhibitor, and human and yellow-tail sera inhibit this enzyme; EDTA and N-tosyl-L-phenylalanylchloromethane are less inhibitory. This enzyme is somewhat activated by cysteine while such sulfhydryl reagents as p-chloromercuribezoate, monoiodoacetate, and N-ethylmaleimide have no effect. This suggests that pyloric caecum collagenase does not require sulfhydryl groups for activity even though it is slightly activated by cysteine.<br> This enzyme activity, as investigated by polyacrylamide disc electrophoresis, results in a marked decrease in the original β-component and the apearance of numerous new components beneath the original α-band.<br> Its mode of attack on collagen and sensitivity to various inhibitors indicate that this enzyme resembles crab hepatopancreas collagenase rather than most known animal collagenases.

収録刊行物

  • 日本水産学会誌

    日本水産学会誌 42 (4), 455-463, 1976

    公益社団法人 日本水産学会

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