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Premium Cyclophilin‐B is an abundant protein whose conformation is similar to cyclophilin‐A
Author(s)
Galat Andrzej,
Bouet Françoise
Publication year1994
Publication title
febs letters
Resource typeJournals
PublisherElsevier BV
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.
Subject(s)biochemistry , biology , biophysics , chemistry , circular dichroism , cyclophilin , cyclophilin a , dna , enzyme , gene , hyperchromicity , isomerase , microbiology and biotechnology , peptidylprolyl isomerase , pin1 , prolyl isomerase
Language(s)English
SCImago Journal Rank1.593
H-Index257
eISSN1873-3468
pISSN0014-5793
DOI10.1016/0014-5793(94)00501-x

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