Cyclophilin-B is an abundant protein whose conformation is similar to cyclophilin-A.
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 NH2-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.
Département d'Ingénierie et d'Etudes des Protéines, D.S.V., C.E.A., C.E. Saclay, Gif-sur-Yvette, France.
A
A
Galat
F
F
Bouet
D000591:Amino Acid Isomerases / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002417:Cattle; D002942:Circular Dichroism; D021983:Cyclophilins; D015180:Electrophoresis, Gel, Two-Dimensional; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase; D011487:Protein Conformation; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013154:Spleen / Q000737:chemistry
D000596:Amino Acids; D002352:Carrier Proteins; C081786:cyclophilin B; D000591:Amino Acid Isomerases; D021983:Cyclophilins; D019696:Peptidylprolyl Isomerase