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. 1994 Jun 15;300 ( Pt 3)(Pt 3):871-5.
doi: 10.1042/bj3000871.

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

S Bose  1 , M Mücke, R B Freedman
Affiliations

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

S Bose et al. Biochem J. .

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.

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