红细胞膜天冬氨酸蛋白酶与组织蛋白酶E之间的生化及免疫化学相似性

Biochemical and immunochemical similarity between erythrocyte membrane aspartic proteinase and cathepsin E.

作者信息

Yamamoto K, Ueno E, Uemura H, Kato Y

机构信息

Department of Pharmacology, Nagasaki University School of Dentistry, Japan.

出版信息

Biochem Biophys Res Commun. 1987 Oct 14;148(1):267-72. doi: 10.1016/0006-291x(87)91105-3.

DOI:10.1016/0006-291x(87)91105-3

PMID:3314869

Abstract

An aspartic proteinase previously thought to be unique to erythrocyte membranes, termed "EMAP", has been shown to be closely related to cathepsin E. Enzymic comparison revealed that these two enzymes resembled each other in molecular weight, susceptibility to pepstatin and chromatographic behaviors on DEAE-Sephacel and Mono P chromatofocusing columns. They were immunoprecipitated by antiserum against human EMAP in a similar way. Immunochemical similarity between the two enzymes was also substantiated by immunoblot analysis.

摘要

一种以前被认为是红细胞膜所特有的天冬氨酸蛋白酶，称为“EMAP”，已被证明与组织蛋白酶E密切相关。酶学比较表明，这两种酶在分子量、对胃蛋白酶抑制剂的敏感性以及在DEAE-琼脂糖凝胶和Mono P聚焦层析柱上的色谱行为方面彼此相似。它们以相似的方式被抗人EMAP抗血清免疫沉淀。免疫印迹分析也证实了这两种酶之间的免疫化学相似性。