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Cyclophilin‐B is an abundant protein whose conformation is similar to cyclophilin‐A
Author(s) -
Galat Andrzej,
Bouet Françoise
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00501-x
Subject(s) - cyclophilin , cyclophilin a , chemistry , cis trans isomerases , peptidylprolyl isomerase , biochemistry , biology , microbiology and biotechnology , enzyme , isomerase , gene
Cyclophilin‐B (bCyP‐20) was isolated in a relatively high quantity from calf brain and spleen tissues consecutively applying weak cation exchange, chromatofocusing and strong cation exchange chromatographies. Edman degradation yielded the N‐terminal sequence NH 2 ‐DEKKKGPKVTVK‐VYFDLRIGDEDIGRVVIGLFGKTVPKTVDNFVAL. Bovine cyclophilin‐B possesses the peptidylproline cis‐trans isomerase activity which is inhibited by nM concentrations of CsA. bCyP‐20 has a strong tendency to bind to cation exchangers including DNA and heparin. It could be released from DNA affinity column at concentrations of NaCl higher than 200 mM. Circular dichroism spectroscopy revealed that bovine cyclophilin‐A (bCyP‐18) and bCyP‐20 in aqueous solution have similar conformations.