| Autor: |
Floderus, Eugenie, Linder, Lars, Sund, Marie-Louise |
| Zdroj: |
Current Microbiology; Aug1990, Vol. 21 Issue 2, p145-149, 5p |
| Abstrakt: |
Extracts of cytoplasmic membranes of Streptococcus sanguis 903 were analyzed for aminopeptidase activity by isoelectric focusing in polyacrylamide gel and enzyme staining with 16 different aminopeptidase substrates. A single aminopeptidase with specificity for aminoterminal arginine was detected. The enzyme was stimulated by dithiothreitol and β-mercaptoethanol. Urea, sodium dodecyl sulfate (SDS), and p-chloromercuribenzoate were inhibitory. Metal ions had little or no effect on activity, except that Hg, Cu, and Ni were inhibitory. The pH optimum for activity was at 7.2. The molecular mass estimated by SDS-polyacrylamide gel electrophoresis was 170 kDa. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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