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Human skeletal muscle proteins

The Primary Structure of Troponin C.

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Summary

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 evolution, one of the most conservative proteins so far studied.

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Author notes

  1. A. E. Romero-Herrera

    Present address: Department of Anatomy, Wayne State University, 48201, Detroit, Michigan, USA

Authors and Affiliations

  1. University Department of Clinical Biochemistry, Addenbrooke's Hospital, Hills Road, CB2 2QR, Cambridge, United Kingdom

    A. E. Romero-Herrera, O. Castillo & H. Lehmann

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  1. A. E. Romero-Herrera
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  2. O. Castillo
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  3. H. Lehmann
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Romero-Herrera, A.E., Castillo, O. & Lehmann, H. Human skeletal muscle proteins. J Mol Evol 8, 251–270 (1976). https://doi.org/10.1007/BF01730999

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  • DOI: https://doi.org/10.1007/BF01730999

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