The characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic-reticulum lumen-Reference-Cited by-同舟云学术

The characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic-reticulum lumen

Published:1994-06-15 Issue:3 Volume:300 Page:871-875
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Bose S¹,Mücke M²,Freedman R B¹

Affiliation:

1. Research School of Biosciences, Biological Laboratory, University of Kent, Canterbury CT2 7NJ, Kent. U.K.

2. Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Federal Republic of Germany

Abstract

A luminally located peptidyl prolyl cis-trans-isomerase (PPI) has been purified from bovine liver microsomes. It has a molecular mass of 20.6 kDa, 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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/300/3/871/613796/bj3000871.pdf

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