title: Primary structure of rabbit skeletal muscle troponin-T. Sequence determination of the NH2-terminal fragment CB3 and the complete sequence of troponin-T.
abstract: The amino acid sequence of CB3, the NH2-terminal fragment of troponin-T, and the alignment of all six cyanogen bromide (CB) fragments are reported. Fragment CB3, comprised of 70 residues, has eight of the nine prolines of troponin-T. As observed in other proteins of the myofibrillar system, its NH2 terminus is blocked by an acetyl group. Methionine-containing "overlap" peptides isolated from a peptic digest of troponin-T as well as 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine cleavage of the protein were used to order the fragments as CB3-CB2-CB5-CB4-CB7-CB6. The complete sequence of troponin-T, a single polypeptide chain of 259 amino acids having a molecular weight of 30,500, is presented.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003488:Cyanogen Bromide; D008970:Molecular Weight; D009124:Muscle Proteins; D009132:Muscles; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D011817:Rabbits; D014336:Troponin
chemical_list: D000596:Amino Acids; D009124:Muscle Proteins; D010446:Peptide Fragments; D014336:Troponin; D010447:Peptide Hydrolases; D010434:Pepsin A; D003488:Cyanogen Bromide