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. 1977 Sep;131(3):891–896. doi: 10.1128/jb.131.3.891-896.1977

Purification of the extracellular protease of Bacillus licheniformis and its inhibition by bacitracin.

L Vitković, H L Sadoff
PMCID: PMC235546  PMID: 893345

Abstract

Sporulating cells of Bacillus licheniformis excrete three seryl proteases that are of similar size, 28,000 daltons, but of different charge at pH 6. The peptide antibiotic bactracin is released from the cells at the same time and exists, in part, as a bacitracin-protease complex that is stable throughout chromatographic procedures employed in enzyme purification. However, preextraction of crude protease with CHCl3 and subsequent gel filtration effect separation of the antibiotic and the enzyme. Three purified, bacitracin-free proteases, designated CMC I, CMC II, and CMC III and whose ratios of total activity are 1:3.7:10.3, respectively, are obtained by chromatography on carboxymethyl cellulose. The major component, CMC III, is inhibited by commercial bacitracin at near-physiological concentrations of the antibiotic.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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