| Literature DB >> 8010972 |
S Bose1, M Mücke, R B Freedman.
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.Entities:
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Year: 1994 PMID: 8010972 PMCID: PMC1138246 DOI: 10.1042/bj3000871
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857