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.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Anderson, C.W., Baum, P.R., Gesteland, R.F. (1973). J.Virol. 12, 241–252
Archer, R., Crocker, C. (1952). Biochim.Biophys.Acta 9, 704–705
Baglioni, C. (1961). Biochim.Biophys.Acta 48, 392–396
Cohen, C. (1975). Sci.Am. 233, 36–45
Collins, J.H., Potter, J.D., Horn, M.J., Wiltshire, G., Jackman, N. (1973). FEBS Letters 36, 268–272
Collins, J.H. (1974). Biochem.Biophys.Res.Comm. 58, 301–308
Dayhoff, M.O. (1972). Atlas of protein sequence and structure: Silver Spring, Maryland: National Biomedical Research Foundation
Doolittle, R.F. (1972). In: Methods in enzymology, C.W. Hirs, S.N. Timasheff, eds., Vol. XXV, pp. 231–244. New York, London: Academic Press
Ebashi, S. (1972). J.Biochem. 72, 787–790
Edman, P. (1956). Acta Chem.Scand. 10, 761–768
Gray, W.R. (1967). In: Methods in enzymology, C.W. Hirs, ed., Vol. XI, pp. 469–475. New York, London: Academic Press
Greaser, M.L., Gergely, J. (1971). J.Biol.Chem. 246, 4226–4233
Greaser, M.L., Yamaguchi, M., Brekke, C., Potter, J., Gergely, J. (1972). Cold Spring Harbor Symp.Quant.Biol. 37, 235–244
Gross, E. (1967). In: Methods in enzymology, C.W. Hirs, ed., Vol. XI, pp. 238–255. New York, London: Academic Press
Hartley, B.S. (1970). Biochem.J. 119, 805–822
Hirs, C.H.W. (1956). J.Biol.Chem. 219, 611–621
Hitchcock, S.E., Huxley, H.E., Szent-Györgyi, A.G. (1973). J.Mol.Biol. 80, 825–836
Huxley, H.E. (1972). Cold Spring Harbor Symp.Quant.Biol. 37, 361–376
Ingram, V.M. (1958). Biochim.Biophys.Acta 28, 539–545
Jepson, J.B., Smith, I. (1953). Nature 172, 1100–1101
Jones, R.T. (1964). Cold Spring Harbor Symp.Quant.Biol. 29, 297–308
Kimura, M. (1969). Proc.Natl.Acad.Sci. 63, 1181–1188
Kretsinger, R.H., Nockolds, C.E. (1973). J.Biol.Chem. 248, 3313–3326
Kretsinger, R.H., Barry, C.D. (1975). Biochim.Biophys.Acta 405, 40–52
Laemmli, U.K. (1970). Nature 227, 680–685
Lorkin, P.A., Charlesworth, D., Lehmann, H., Rahbar, S., Tuchinda, S., Lie-Injo Luang Eng (1970). Brit.J.Haematol. 19, 117–125
Moews, P.C., Kretsinger, R.H. (1975). J.Mol.Biol. 91, 201–228
Naughton, M.A., Hagopian, H. (1962). Anal.Biochem. 3, 276–284
Needham, D.M. (1971). Machina carnis. Cambridge: University Press
Offord, R.E. (1966). Nature 211, 591–593
Pechère, J.F. (1974). C.R.Acad.Sci.(Paris) 278D, 2577–2579
Potter, J.D., Gergely, J. (1975). J.Biol.Chem. 250, 4628–4633
Sanger, F., Tuppy, H. (1951). Biochem.J. 49, 463–481
Sciarratta, G.V., Centa, A. (1970). Soluzioni. 1, 4–5
Sick, K., Beale, D., Irvine, D., Lehmann, H., Goodall, P.T., MacDougall, S. (1967). Biochim.Biophys.Acta 140, 231–242
Smith, I. (1953). Nature 171, 43–44
Smith, I., Seakins, J.W.T., Dayman, J. (1969). In: Chromatographic and electrophoretic techniques, I. Smith, ed., Vol. I, pp. 149–150. London: William Heinemann Med.Books
Toennies, G., Kolb, J.J. (1951). Anal.Chem. 23, 823–826
Tufty, R.M., Kretsinger, R.H. (1975). Science 187, 167–169
Van Eerd, J.P., Takahashi, K. (1975). Biochem.Biophys.Res.Comm. 64, 122–127
Weeds, A.G., Mclachlan, A.D. (1974). Nature 252, 646–649
Wittenberg, J.B. (1970). Physiol.Rev. 50, 559–635
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01730999