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凡纳滨对虾(甲壳纲,十足目)中一种具有胰凝乳蛋白酶和胶原酶活性的丝氨酸蛋白酶的纯化、生化特性及N端序列分析

Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda).

作者信息

Van Wormhoudt A, Le Chevalier P, Sellos D

机构信息

Laboratoire de Biologie Marine, Collège de France, Concarneau.

出版信息

Comp Biochem Physiol B. 1992 Nov;103(3):675-80. doi: 10.1016/0305-0491(92)90389-9.

DOI:10.1016/0305-0491(92)90389-9
PMID:1458841
Abstract
  1. Two chymotrypsin variants, with collagenolytic activities, were purified from the hepatopancreas of Penaeus vannamei using radioactive protein as the substrate. 2. These proteases are very close as far as amino acid composition, molecular weight, inhibitors studies and specificity against small synthetic substrates are concerned. 3. N-terminal amino acid sequences of both variants are identical and are very close to other known crustacean serine proteases.
摘要
  1. 以放射性蛋白质为底物,从凡纳滨对虾的肝胰腺中纯化出两种具有胶原分解活性的胰凝乳蛋白酶变体。2. 就氨基酸组成、分子量、抑制剂研究以及对小合成底物的特异性而言,这些蛋白酶非常相似。3. 两种变体的N端氨基酸序列相同,且与其他已知的甲壳类丝氨酸蛋白酶非常接近。

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