
Protein phosphorylation in Streptomyces albus
Author(s) -
Dobrová Z.,
Jiršsová M.,
Petřík T.,
Ryšavý P.,
Náprstek J.,
Janeček J.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03813.x
Subject(s) - phosphorylation , streptomyces albus , biochemistry , protein kinase a , in vitro , protein phosphorylation , kinase , gel electrophoresis , biology , substrate level phosphorylation , in vivo , microbiology and biotechnology , chemistry , streptomyces , bacteria , genetics
The phosphorylated proteins of Streptomyces albus , radioactively labeled with [ 32 P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 proteins species were found to be phosphorylated. With [ 32 P]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.