title: Cyclosporin A sensitive peptidyl-prolyl cis-trans isomerase in a halophilic archaeum, Halobacterium cutirubrum.
abstract: A cyclophilin type peptidyl-prolyl cis-trans isomerase was purified from a halophilic archaeum, Halobacterium cutirubrum DSM 669. The activity increased with an increase in KCl concentration up to 4 M. Sensitivity to cyclosporin A was comparable to that of eukaryotic cyclophilin and was also affected by KCl. IC50 for Cyclosporin A was 1.5 x 10(-8) M in 2.9 M KCl but 1.4 x 10(-7) M in 1.4 M KCl. The apparent molecular weight was 31 K by SDS-PAGE and 22 K in 2.9 M KCl and 150 K in 0 M KCl by gel filtration chromatography. The N-terminal amino acid sequence (33 residues) sheared 4 completely and 5 highly conserved amino acid residues with other reported cyclophilin family PPIases.
authors.affiliation: Marine Biotechnology Institute, Shimizu Laboratories, Shizuoka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Nagashima
authors.forename: S
authors.initials: S
authors.lastname: Mitsuhashi
authors.forename: K
authors.initials: K
authors.lastname: Kamino
authors.forename: T
authors.initials: T
authors.lastname: Maruyama
mesh_terms: D000591:Amino Acid Isomerases / Q000187:drug effects* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000187:drug effects* / Q000302:isolation & purification*; D016572:Cyclosporine / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D006217:Halobacterium / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019696:Peptidylprolyl Isomerase; D011189:Potassium Chloride / Q000494:pharmacology; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000494:pharmacology
chemical_list: D002352:Carrier Proteins; D012965:Sodium Chloride; D011189:Potassium Chloride; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase