| Autor: |
Floderus, Eugenie, Linder, Lars E., Sund, Marie-Louise |
| Zdroj: |
Current Microbiology; August 1990, Vol. 21 Issue: 2 p145-149, 5p |
| Abstrakt: |
Extracts of cytoplasmic membranes ofStreptococcus 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 andβ-mercaptoethanol. Urea, sodium dodecyl sulfate (SDS), andp-chloromercuribenzoate were inhibitory. Metal ions had little or no effect on activity, except that Hg2+, Cu2+, and Ni2+ were inhibitory. The pH optimum for activity was at 7.2. The molecular mass estimated by SDS-polyacrylamide gel electrophoresis was 170 kDa. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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