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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Isomerases / antagonists & inhibitors
  • Amino Acid Isomerases / immunology
  • Amino Acid Isomerases / isolation & purification*
  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / immunology
  • Carrier Proteins / isolation & purification*
  • Cattle
  • Cyclosporine / pharmacology
  • Endoplasmic Reticulum / enzymology*
  • Kinetics
  • Molecular Sequence Data
  • Peptidylprolyl Isomerase
  • Protein Conformation
  • Substrate Specificity

Substances

  • Carrier Proteins
  • Cyclosporine
  • Amino Acid Isomerases
  • Peptidylprolyl Isomerase