Skip to main content
Log in

On the cysteine and cystine content of proteins

Differences between Intracellular and Extracellular Proteins

  • Published:
Journal of Molecular Evolution Aims and scope Submit manuscript

Summary

Analysis of published data on the cysteine and half-cystine content of proteins indicates that most intracellular proteins may be classified as sulfhydryl proteins (those containing cysteine but little or no half-cystine) and that such sulf-hydryl proteins have a low cysteine content. The mean cysteine content found for 32 intracellular mammalian proteins was 1.6 % and intracellular proteins of many bacteria have similar or lower values. Extracellular mammalian proteins are primarily disulfide proteins (those containing half-cystine but little or no cysteine) and have a high half-cystine content, the mean value found for some 34 extracellular mammalian proteins being 4.1 %. This is contrasted with many of the extracellular proteins from facultative bacteria which are cyst(e)ine-free proteins, being lacking in both cysteine and half-cystine. These and related observations are interpreted in terms of the evolution of life in a reducing atmosphere and the subsequent transition to an oxidizing environment. It is suggested that disulfide proteins evolved primarily after the accumulation of oxygen in the atmosphere.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Banaszak, L.J., Bradshaw, R.A., (1975). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XI, p. 369. New York: Academic Press

    Google Scholar 

  • Barron, E.S.G., Singer, T.P. (1943). Science97, 356

    Google Scholar 

  • Bieber, H., Zimmermann, W., (1971). Zbl. Bakt., I. Abt. Orig.217, 47

    Google Scholar 

  • Dickerson, R.E., Timkovitch, R. (1975). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XI, p. 397. New York: Academic Press

    Google Scholar 

  • Friedman, M. (1973). The chemistry and biochemistry of the sulfhydryl group in amino acids., peptides and proteins. New York: Pergamon Press

    Google Scholar 

  • Gatlin, L.L. (1974). J. Mol. Evol.3, 189

    Google Scholar 

  • Gatlin, L.L. (1976). J. Mol. Evol.7, 185

    Google Scholar 

  • Gertler, A., Trop, M. (1971). Eur. J. Biochem.19, 90

    Google Scholar 

  • Harper, E., Seifter, S. (1974). Isr. J. Chem.12, 515

    Google Scholar 

  • Harris, J. I., Waters, M. (1976). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XIII, p. 1. New York: Academic Press

    Google Scholar 

  • Haugaard, N. (1968). Physiol. Rev.48, 311

    Google Scholar 

  • Holmquist, R. (1975). J. Mol. Evol.4, 277

    Google Scholar 

  • Jocelyn, P.C. (1972). Biochemistry of the SH Group, Chapt. 1. New York: Academic Press

    Google Scholar 

  • Jukes, T.H., Holmquist, R., and Moise, H. (1975). Science,189, 50

    Google Scholar 

  • Kimura, M. (1968). Genet. Res., Camb.11, 247

    Google Scholar 

  • King, J.L., Jukes, T.H. (1969). Science164, 788

    Google Scholar 

  • Liu, T.Y., Elliott, S.D. (1971). The enzymes, P.D. Boyer, ed., Vol. III, p. 609. New York: Academic Press

    Google Scholar 

  • Malkin, R. (1973). Iron-Sulfur Proteins, W. Lovenberg, ed., Vol. II, p. 1. New York: Academic Press

    Google Scholar 

  • Markland, Jr., F.S., Smith, E.L. (1971). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. III p. 561. New York: Academic Press

    Google Scholar 

  • Matsubara, H., Feder, J. (1971). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. III, p. 721. New York: Academic Press

    Google Scholar 

  • Miller, T.E., Stone, R.W. (1938). J. Bacteriol.36, 248

    Google Scholar 

  • Mitchell, W.M., Harrington, W.F. (1968). J. Biol. Chem.243, 4683

    Google Scholar 

  • Murphey, W.H., Barnaby, C., Lin, F.J. and Kaplan, N.O. (1967). J. Biol. Chem.242, 1548

    Google Scholar 

  • Ohta, T., Kimura, M. (1971). Science174, 150

    Google Scholar 

  • Olafson, R.W., Jurasek, L., Carpenter, M.R., and Smillie, L.B. (1975). Biochemistry14, 1168

    Google Scholar 

  • Olson, M.O.J., Nagabhushan, N., Dzwinill, M., Smillie, L.B., and Whitaker, D.R. (1970). Nature228, 438

    Google Scholar 

  • Pollock, M.R., (1962). The bacteria, I.C. Gunsalas, R.Y. Stanier, eds., Vol. IV, p. 121. New York: Academic Press

    Google Scholar 

  • Pollock, M.R., Richmond, M.H. (1962). Nature194, 446

    Google Scholar 

  • Reddy, M.N., Keim, P.S., Heinrikson, R.L., Kezdy, R.J. (1975). J. Biol. Chem.250, 1741

    Google Scholar 

  • Reeck, G.R., (1970). Handbook of biochemistry, H.A. Sober, ed., 2nd ed., p. C282. Cleveland: Chemical Rubber Company

    Google Scholar 

  • Reeck, G.R., Fisher, L. (1973). Int. J. Peptide Res.5, 109

    Google Scholar 

  • Rosenberg, S.A., Guidotti, G. (1968). J. Biol. Chem.243, 1985

    Google Scholar 

  • Saheb, S.A. (1976). Biochimie58, 793

    Google Scholar 

  • Smith, M.H. (1966). J. Theoret. Biol.13, 261

    Google Scholar 

  • Williams, Jr., C.H. (1976). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XIII, p. 90. New York: Academic Press

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Fahey, R.C., Hunt, J.S. & Windham, G.C. On the cysteine and cystine content of proteins. J Mol Evol 10, 155–160 (1977). https://doi.org/10.1007/BF01751808

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01751808

Key words

Navigation