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JBC, Vol. 252, Issue 3, 983-989, Feb, 1977

Primary structure of rabbit skeletal muscle troponin-T. Sequence determination of the NH2-terminal fragment CB3 and the complete sequence of troponin-T

J. R. Pearlstone, P. Johnson, M. R. Carpenter and L. B. Smillie

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.
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