title: Structural analysis of cGMP-dependent protein kinase using limited proteolysis.
abstract: cGMP-dependent protein kinase from bovine lung is labile to specific proteolysis. Limited digestion with chymotrypsin produces a 65,000-dalton monomer and a 16,000-dalton dimer from a 150,000-dalton dimeric enzyme. The larger proteolytic fragment represents the COOH-terminal portion of the enzyme and contains the catalytic site along with the cGMP binding site. The smaller fragment representing the NH2-terminal portion of the enzyme contains the autophosphorylation site and the interchain disulfide bond(s). A model defining the functional domains of cGMP-dependent protein kinase is presented and comparisons with cAMP-dependent protein kinase regulatory subunit are discussed.
mesh_terms: D000818:Animals; D002417:Cattle; D002918:Chymotrypsin; D006152:Cyclic GMP / Q000494:pharmacology*; D004789:Enzyme Activation; D008168:Lung / Q000201:enzymology; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D011494:Protein Kinases; D002918:Chymotrypsin; D014357:Trypsin; D006152:Cyclic GMP