作者: Barton Holmquist
DOI: 10.1021/BI00640A009
关键词: Gel electrophoresis 、 Thermolysin 、 Zinc 、 Bacillus cereus 、 Protease 、 Affinity chromatography 、 Amino acid 、 Chemical modification 、 Chromatography 、 Chemistry
摘要: The neutral protease isolated from Bacillus cereus (BRL-70) has been purified by affinity chromatography and characterized. enzyme exhibits a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, molecular weight of 34 000 ultracentrifugation, contains one enzymatically essential zinc atom per g. These data together with the amino acid composition, response to metal substitution, chemical modification, substrate specificity all indicate that this is monomeric typical bacterial metalloprotease.