THE CHARACTERIZATION OF A CYCLOPHILIN-TYPE PEPTIDYL-PROLYL CIS-TRANS-ISOMERASE FROM THE ENDOPLASMIC-RETICULUM LUMEN

被引：30

作者：

BOSE, S ^{[1
]}

MUCKE, M ^{[1
]}

FREEDMAN, RB ^{[1
]}

机构：

[1] UNIV BAYREUTH,BIOCHEM LAB,D-95440 BAYREUTH,GERMANY

来源：

BIOCHEMICAL JOURNAL | 1994年 / 300卷

关键词：

D O I：

10.1042/bj3000871

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

A luminally located peptidyl prolyl cis-trans-isomerase (PPI) has been purified from bovine liver microsomes. It has a molecular mass of 20.6kDa, and N-terminal sequencing demonstrates strong sequence similarity to the sequences of the cyclophilin B family. The enzyme catalyses the isomerization of the standard proline-containing peptide N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide, as well as the refolding of RNAase T1. Kinetic properties, substrate-specificity data and inhibition by cyclosporin A indicate that it is a cyclophilin-type PPI, consistent with the amino-acid-sequence results.

引用

页码：871 / 875

页数：5

共 32 条

[1]

S-CYCLOPHILIN IS RETAINED INTRACELLULARLY VIA A UNIQUE COOH-TERMINAL SEQUENCE AND COLOCALIZES WITH THE CALCIUM STORAGE PROTEIN CALRETICULIN [J].