Protein phosphorylation in Streptomyces albus

The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous prote...

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Bibliographic Details
Published inFEMS microbiology letters Vol. 59; no. 1-2; p. 145
Main Authors Dobrová, Z, Jiresová, M, Petrík, T, Rysavý, P, Náprstek, J, Janecek, J
Format Journal Article
LanguageEnglish
Published England 01.09.1990
Subjects
Bacterial Proteins - metabolism
Electrophoresis, Polyacrylamide Gel
Molecular Weight
Phosphorylation
Protein Kinases - isolation & purification
Protein Kinases - metabolism
Streptomyces - enzymology
Streptomyces - metabolism
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Summary:The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous proteins in vitro which were predominantly phosphorylated in vivo. From cell extract which exhibited active phosphorylated in vitro, a protein kinase has been partially purified. The kinase activity was identified in fractions corresponding to a 90 kDa protein.
ISSN:0378-1097
DOI:10.1111/j.1574-6968.1990.tb03813.x