Isolation of mitochondrial cyclophilin from bovine heart.
Peptidyl-Prolyl cis-trans isomerase was isolated from bovine heart mitochondrial matrix. The enzyme has a M(r) of 19,000 and its activity was inhibited by cyclosporin A (inhibition constant, 6.9 nM), but not by FK-506. The mitochondrial content of the enzyme is in good agreement with the number of binding sites for cyclosporin A (85 pmol/mg of matrix protein). Partial amino acid sequencing showed that the enzyme has a serine-rich N-terminal extension and is similar to human cyclophilin 3 (Bergsma et al. (1991) J. Biol. Chem. 266, 23204-23214) rather than the cytosolic and endoplasmic reticulum isoforms. We conclude that this protein is mitochondrial cyclophilin and a homologue of human cyclophilin 3.
Inoue
T
T
Department of Physiological Chemistry, Osaka University Medical School, Suita, Japan.
Yoshida
Y
Y
Isaka
Y
Y
Tagawa
K
K
D000591:Amino Acid Isomerases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D016572:Cyclosporine / Q000494:pharmacology; D008929:Mitochondria, Heart / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus / Q000494:pharmacology
D002352:Carrier Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus