Human skeletal muscle proteins. The primary structure of troponin C.
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Romero-Herrera AE, Castillo O, Lehmann H
Human skeletal muscle proteins. The primary structure of troponin C.
J Mol Evol. 1976 Oct 27;8(3):251-70.
- PubMed ID
- 978749 [ View in PubMed]
- Abstract
The primary structure of the major component of human skeletal muscle troponin C has been established. The troponin C was purified by ammonium sulphate and isoelectric fractionation, followed by two chromatographic steps on DEAE Sephadex. The sequence was determined from the different overlapping enzymic peptides and by dansyl-Edman degradation. The only difference between rabbit skeletal muscle troponin C and the major component of human skeletal troponin C was found at position 112: Ala (rabbit), Pro (human). The partial amino acid sequence of the first 86 residues of the minor component of human skeletal troponin C was found to resemble the troponin C from bovine cardiac muscle. The only difference between them, has tentatively been located at position 62: Glu (human), Asp (bovine). These similarities suggest that troponin C is, from the point of view of molecular, one of the most conservative proteins so far studied.