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大鼠皮肤组织蛋白酶D的纯化及生化特性研究

Purification and biochemical characterization of rat skin cathepsin D.

作者信息

Heikkinen J E, Järvinen M, Jansén C R

出版信息

J Invest Dermatol. 1975 Sep;65(3):272-8. doi: 10.1111/1523-1747.ep12598339.

Abstract

The hemoglobin-hydrolyzing, acidic proteinase activity of rat skin was purified by using ammonium sulfate precipitation. Sephadex G-100 gel column chromatography, acid treatment, and DEAE-cellulose column chromatography, giving a purification coefficient of 182. The pH optimum, molecular size, substrate specificity, as well as inhibitor and activator sensitivity of the enzyme preparation, corresponded closely to those of cathepsin D. The enzyme activity was separated from cathepsin B1. The present status of the knowledge of skin cathespins is reviewed.

摘要

通过硫酸铵沉淀、Sephadex G - 100凝胶柱色谱、酸处理和DEAE - 纤维素柱色谱法,对大鼠皮肤的血红蛋白水解酸性蛋白酶活性进行了纯化,纯化系数为182。该酶制剂的最适pH、分子大小、底物特异性以及对抑制剂和激活剂的敏感性与组织蛋白酶D密切相关。该酶活性与组织蛋白酶B1分离。本文综述了皮肤组织蛋白酶的知识现状。

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