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JBC, Vol. 252, Issue 3, 983-989, Feb, 1977
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.
Primary structure of rabbit skeletal muscle troponin-T. Sequence determination of the NH2-terminal fragment CB3 and the complete sequence of troponin-T
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