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J Antibiot (Tokyo). 1980 Dec;33(12):1551-5.

Selective cleavage of a peptide antibiotic, colistin by colistinase.


A colistin-inactivating enzyme, colistinase was produced by Bacillus polymyxa var. colistinus KOYAMA, a colistin-producing microorganism. The crude colistinase was fractionated as two components (colistinase I and II) by Sephadex G-50 gel filtration. Colistinase II was further purified and then, it showed as a single band in polyacrylamide disc gel electrophoresis. The molecular weight of colistinase II was about 20,000 by Sephadex G-100 gel filtration and the isoelectric point was at about 8.3. Colistinase II cleaved specifically between the 2,4-diaminobutyric acid of the side chain and 2,4-diaminobutyric acid adjacent in the cyclic peptide portion of colistin molecule.

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