兔骨骼肌半胱氨酸蛋白酶抑制剂。

M Matsuishi, A Okitani, Y Hayakawa, H Kato
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引用次数: 13

摘要

1. 从兔骨骼肌中分离出两种半胱氨酸蛋白酶抑制剂I-T (Mr = 29,000)和I-S (Mr = 10,700),分别采用中性缓冲液提取、pH = 3.7沉淀、丙酮分馏和Sephadex G-75凝胶渗透等方法。2. I-T是单体抑制剂I-M (Mr = 10,500)通过二硫键形成的三聚体。3.I-S在pH 3 ~ 8之间几乎完全稳定,而I-M在相同的pH范围内则不稳定。4. I-M对组织蛋白酶H和L的作用最有效,对组织蛋白酶B的活性中等,对木瓜蛋白酶的活性较弱。I-S对组织蛋白酶L的作用最有效,其次是组织蛋白酶H、组织蛋白酶B和木瓜蛋白酶。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Cysteine proteinase inhibitors from rabbit skeletal muscle.

1. Two cysteine proteinase inhibitors, I-T (Mr = 29,000) and I-S (Mr = 10,700), were isolated from rabbit skeletal muscle by means of succesive extraction with a neutral buffer solution, precipitation at pH 3.7, acetone fractionation and gel permeation on Sephadex G-75. 2. I-T is a formed trimer of a monomeric inhibitor, I-M (Mr = 10,500), through disulfide bonds. 3. I-S is almost completely stable between pH 3 and 8, while I-M is unstable in the same pH range. 4. I-M acts most effectively towards cathepsins H and L, showing moderate activity towards cathepsin B and only weak activity towards papain. I-S acts most effectively towards cathepsin L, followed by, in decreasing order, cathepsin H, cathepsin B and papain.

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