| Autor: |
Spencer, D B, Hansa, J G, Stuckmann, K V, Hulett, F M |
| Zdroj: |
Journal of Bacteriology; May 1982, Vol. 150 Issue: 2 p826-834, 9p |
| Abstrakt: |
When membranes of Bacillus licheniformis MC14 were extracted exhaustively with 1 M magnesium, approximately 80% of the membrane-associated alkaline phosphatase (orthophosphoric-monoester phosphohydrolase [alkaline optimum], E.C. 3.1.3.1) was solubilized. The remaining activity could be extracted with a cationic detergent, hexadecylpyridinium chloride, without loss of enzymatic activity. The detergent-extractable alkaline phosphatase was immunoprecipitable with antibody to the salt-extractable alkaline phosphatase or the secreted alkaline phosphatase, had an approximate molecular weight of 60,000, and was localized 100% on the outer surface of the cytoplasmic membrane. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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