Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
FEMS microbiology letters
133 (1995), S. 0
ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract Transfer of phosphate from γ-[32P]ATP to endogenous proteins catalysed by cell-free extracts was used as a tool for studies of protein phosphorylation via protein kinases in streptomycetes. Thus, phosphoproteins were detected in submerged spores and vegetative mycelium of Streptomyces granaticolor which were identified as O-phosphomonoesters rather than N-phosphates or acyl phosphates. The extent and pattern of phosphorylation was dependent on the growth stage of the culture and was greatly enhanced by Mn2+.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1995.tb07866.x
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