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  • Title: Cyclosporin A sensitive peptidyl-prolyl cis-trans isomerase in a halophilic archaeum, Halobacterium cutirubrum.
    Author: Nagashima K, Mitsuhashi S, Kamino K, Maruyama T.
    Journal: Biochem Biophys Res Commun; 1994 Jan 28; 198(2):466-72. PubMed ID: 8297356.
    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.
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