Comparison of the substrate specificity of adenosine 3':5'-monophosphate- and guanosine 3':5'-monophosphate-dependent protein kinases. Kinetic studies using synthetic peptides corresponding to phosphorylation sites in histone H2B.
Glass, D B
Comparison of the substrate specificity of adenosine 3':5'-monophosphate- and guanosine 3':5'-monophosphate-dependent protein kinases. Kinetic studies using synthetic peptides corresponding to phosphorylation sites in histone H2B. [electronic resource] - The Journal of biological chemistry Oct 1979 - 9728-38 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0021-9258
Amino Acid Sequence
Animals
Cattle
Cyclic AMP--pharmacology
Cyclic GMP--pharmacology
Histones
Hydrogen-Ion Concentration
Kinetics
Lung--enzymology
Peptide Fragments
Phosphorylation
Protein Kinases--isolation & purification
Substrate Specificity
Comparison of the substrate specificity of adenosine 3':5'-monophosphate- and guanosine 3':5'-monophosphate-dependent protein kinases. Kinetic studies using synthetic peptides corresponding to phosphorylation sites in histone H2B. [electronic resource] - The Journal of biological chemistry Oct 1979 - 9728-38 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0021-9258
Amino Acid Sequence
Animals
Cattle
Cyclic AMP--pharmacology
Cyclic GMP--pharmacology
Histones
Hydrogen-Ion Concentration
Kinetics
Lung--enzymology
Peptide Fragments
Phosphorylation
Protein Kinases--isolation & purification
Substrate Specificity