The characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic-reticulum lumen
Keyword(s):
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.
1986 ◽
Vol 261
(22)
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pp. 10021-10024
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1986 ◽
Vol 261
(19)
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pp. 8811-8816
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1990 ◽
Vol 265
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pp. 4583-4591
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1992 ◽
Vol 267
(3)
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pp. 1858-1863
1993 ◽
Vol 90
(11)
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pp. 5302-5306
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2000 ◽
Vol 203
(22)
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pp. 3411-3423
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2003 ◽
Vol 15
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pp. 119-122
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