A SEVENTEEN KILODALTONS PEPTIDYL-PROLYL CIS-TRANS ISOMERASE OF THE CYCLOSPORIN-PRODUCER Tolypocladium inflatum IS SENSITIVE TO CYCLOSPORIN A

RAINER ZOCHER; ULLRICH KELLER; CHAN LEE; KAI HOFFMANN

doi:10.7164/antibiotics.45.265

The Journal of Antibiotics

Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820

A SEVENTEEN KILODALTONS PEPTIDYL-PROLYL CIS-TRANS ISOMERASE OF THE CYCLOSPORIN-PRODUCER Tolypocladium inflatum IS SENSITIVE TO CYCLOSPORIN A

RAINER ZOCHER, ULLRICH KELLER, CHAN LEE, KAI HOFFMANN

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JOURNAL FREE ACCESS

1992 Volume 45 Issue 2 Pages 265-268

DOI https://doi.org/10.7164/antibiotics.45.265

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Abstract

A peptidyl-prolyl cis-trans isomerase (PPIase) was purified to homogeneity about 24-fold from the cyclosporin-producing fungus Tolypocladium inflatum. The molecular mass of the enzyme was in the range of 17 kdaltons. Remarkably, the enzyme could be inhibited by cyclosporin A in the nanomolar range as has been shown for numerous other cyclophilins from eukaryotic organisms. This indicates, that Tolypocladium inflatum must possess a self protection system in order to survive in the presence of cyclosporin.

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