Phospholipases of Bacillus Cereus: Further Characterization
Abstract
Results obtained by polyacrylamide gel electrophoresis support the hypothesis that the hydrolyses of phosphatidyl ethanolamine and phosphatidyl choline by the phospholipases C of Bacillus cereus are catalyzed by the same protein, which may be present as isoenzymes. Phosphatidyl inositol and sphingomyelin are hydrolyzed by separate phospholipases that are distinct from the above. Phosphatidyl serine and what appears to be diphosphatidyl inositol are also split by the phospholipases of B. cereus. The yield of phospholipases is much greater in cultures grown statically than in shaken cultures. Zinc and 2-mercaptoethanol had only slight effects on the enzymes specific for phosphatidyl inositol and sphingomyelin, but markedly stimulated phosphatidyl ethanolamine and phosphatidyl choline hydrolysis in a crude preparation of the phospholipases that had been dialyzed against ethylenediaminetetraacetate. A simple microanalytical test has been developed for the detection of phospholipase activity.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 1969
- Accession Number
- AD0848734
Entities
People
- Gerald F. Logan Jr.
- Milton W. Slein