PEPTIDYL-PROLYL CIS-TRANS-ISOMERASE ACTIVITY ASSOCIATED WITH THE LUMEN OF THE ENDOPLASMIC-RETICULUM

被引：23

作者：

BOSE, S

FREEDMAN, RB

机构：

[1] Research School of Biosciences, Bioiogical Laboratory, University of Kent

来源：

BIOCHEMICAL JOURNAL | 1994年 / 300卷

关键词：

D O I：

10.1042/bj3000865

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Peptidyl prolyl cis-trans-isomerase (PPI) activity was detected in microsomal fractions from bovine and rat liver. Extensive washing, proteinase and sonication treatments indicated that although some of this activity was due to adsorbed cytosolic enzymes, there was also an active but latent microsomal PPI activity. Density-gradient subfractionation indicated that activity was associated with vesicles derived from both the rough and the smooth endoplasmic reticulum (ER), suggesting that the activity was located within the ER lumen. The luminal PPI activity was inhibited by cyclosporin A and was active towards an unfolded protein substrate as well as towards the standard peptide substrate.

引用

页码：865 / 870

页数：6

共 39 条

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