Protein phosphorylation in Streptomyces albus
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu časopisecké články
- MeSH
- bakteriální proteiny metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- fosforylace MeSH
- molekulová hmotnost MeSH
- proteinkinasy izolace a purifikace metabolismus MeSH
- Streptomyces enzymologie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- proteinkinasy MeSH
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.
Citace poskytuje Crossref.org
Evidence for phosphoprotein phosphatase in Streptomyces granaticolor
Constitution of the metabolic type of streptomycetes during the first hours of cultivation
Effect of protein phosphorylation on the activity of RNA polymerase in streptomycetes