Characterization of membrane-associated arginine aminopeptidase inStreptococcus sanguis 903

Autor:	Eugenie Floderus, Lars E. Linder, Marie-Louise Sund
Rok vydání:	1990
Předmět:	Gel electrophoresis Arginine Molecular mass Chemistry Isoelectric focusing General Medicine Applied Microbiology and Biotechnology Microbiology Aminopeptidase Molecular biology chemistry.chemical_compound Aminopeptidase B Biochemistry Sodium dodecyl sulfate Polyacrylamide gel electrophoresis
Zdroj:	Current Microbiology. 21:145-149
ISSN:	1432-0991 0343-8651
Popis:	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:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::b077b859f70512f4483d41cff92f3c3d https://doi.org/10.1007/bf02091833 Zobrazit plný text záznamu Full text from SpringerLink