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: | 05 Nov 2024 09:57 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/20395 (The current URI for this page, for reference purposes) |
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