Characterization of the "microprotease" from Bacillus cereus. A zinc neutral endoprotease

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Abstract
The neutral protease isolated from B. cereus (BRL-70) was purified by affinity chromatography and characterized. The enzyme exhibits a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, has a MW of 34,000 by ultracentrifugation, and contains 2 enzymatically essential Zn atom/34,000 g. These data together with the amino acid composition, response to metal substitution, chemical modification and substrate specificity indicate that this protease is monomeric and is a typical bacterial neutral metalloprotease.
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