Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3',5'-phosphate dependent protein kinase.
The 350-residue amino acid sequence of the catalytic subunit of bovine cardiac muscle adenosine cyclic 3',5'-phosphate dependent protein kinase is described. The protein has a molecular weight of 40 862, which includes an N-tetradecanoyl (myristyl) group blocking the NH2 terminus and phosphate groups at threonine-197 and serine-338. Seven methionyl bonds in the S-carboxymethylated protein were cleaved with cyanogen bromide to yield eight primary peptides. These fragments, and subpeptides generated by cleavage with trypsin, pepsin, chymotrypsin, thermolysin, and Myxobacter AL-1 protease II, were purified and analyzed to yield the majority of the sequence. The primary peptides were aligned by analyses of overlapping peptides, particularly of methione-containing tryptic peptides generated after in vitro [14C]methyl exchange labeling of methionyl residues in the intact protein.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D000242:Cyclic AMP / Q000494:pharmacology; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D011494:Protein Kinases / Q000378:metabolism
D046911:Macromolecular Substances; D010446:Peptide Fragments; D000242:Cyclic AMP; D011494:Protein Kinases; D003488:Cyanogen Bromide