Abstract
The effect of cyclic AMP on protein phosphorylation was analyzed comparatively in two strains of E.coli differing in their capacity to synthesize this nucleotide, one of them lacking the adenylate cyclase activity. The results obtained from both in vivo and in vitro experiments concurred in showing that the bacterial protein kinase activity is cAMP-independent.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Cyclic AMP / pharmacology*
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Cyclic GMP / pharmacology
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Kinetics
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Molecular Weight
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Mutation
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Phosphates / metabolism
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Phosphorus Radioisotopes
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Phosphorylation
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Protein Kinases / metabolism*
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Species Specificity
Substances
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Bacterial Proteins
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Phosphates
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Phosphorus Radioisotopes
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Cyclic AMP
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Protein Kinases
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Cyclic GMP