Adenosine cyclic 3',5'-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit
- 9 November 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (23) , 5794-5799
- https://doi.org/10.1021/bi00266a011
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Kinetic studies to determine the mechanism of regulation of bovine liver glutamate dehydrogenase by nucleotide effectorsBiochemistry, 1982
- Nuclear magnetic resonance studies of the conformation and kinetics of the peptide-substrate at the active site of bovine heart protein kinaseBiochemistry, 1981
- Magnetic resonance measurements of intersubstrate distances at the active site of protein kinase using substitution-inert cobalt(III) and chromium(III) complexes of adenosine 5'-(.beta.,.gamma.-methylenetriphosphate)Biochemistry, 1980
- Adenosine 3′,5′-monophosphate-dependent protein kinase: Interaction with guanidinium compoundsArchives of Biochemistry and Biophysics, 1980
- Stereochemical and kinetic studies on the action of the catalytic subunit of bovine cardiac muscle adenosine 3',5'-monophosphate dependent protein kinase using metal ion complexes of ATP.beta.SBiochemistry, 1980
- Phosphorylation of hydroxyproline in a synthetic peptide catalyzed by cyclic AMP-dependent protein kinase.Journal of Biological Chemistry, 1979
- Mapping the ATP-Binding Site in the Catalytic Subunit of A denosine-3':5'-monophosphate-Dependent Protein Kinase. Spatial Relationship with the ATP Site of the Undissociated EnzymeEuropean Journal of Biochemistry, 1978
- The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liverBiochemical and Biophysical Research Communications, 1976