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The Characterization of a Cyclophilin-Type Peptidyl-Prolyl CIS-Trans-Isomerase from the Endoplassimc-Retticulum Lumen

Bose, S., Mucke, M., Freedman, Robert B. (1994) The Characterization of a Cyclophilin-Type Peptidyl-Prolyl CIS-Trans-Isomerase from the Endoplassimc-Retticulum Lumen. Biochemical Journal, 300 . pp. 871-875. ISSN 0264-6021. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:20395)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.

Abstract

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.

Item Type: Article
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: P. Ogbuji
Date Deposited: 26 Aug 2009 20:18 UTC
Last Modified: 16 Nov 2021 09:58 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/20395 (The current URI for this page, for reference purposes)

University of Kent Author Information

Freedman, Robert B..

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