Skip to main content
SpringerLink
Log in

Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

The conformational properties and stability of reduced hen egg lysozyme and those of the disulfide intermediates species formed during renaturation of reduced lysozyme have been reviewed. This information and that related with RNase A and other proteins are interpreted to outline a possible mechanism of renaturation of the reduced protein.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Anfinsen, C. B., 1973. Science 181: 223–230.

    Google Scholar 

  2. Epstein, C. J., Goldberger, R. F. & Anfinsen, C. B., 1963. Cold Spring Harbour Symp. Quant. Biol. 28: 439–449.

    Google Scholar 

  3. Anfinsen, C. B., Haber, E., Sela, M. & White, F. H., Jr., 1961. Proc. Natl. Acad. Sci. U.S.A. 47: 1309–1314.

    Google Scholar 

  4. Epstein, C. J., Goldberger, R. F., Young, D. M. & Anfinsen, C. B., 1962. Arch. Biochem. Biophys. (Suppl. 1): 223–231.

  5. Anfinsen, C. B., 1967. Harvey Lect. 61: 95–116.

    Google Scholar 

  6. Givol, D., Goldberger, R. F. & Anfinsen, C. B., 1964. J. Biol. Chem. 234: 1459–1465.

    Google Scholar 

  7. Venetianer, P. & Straub, F. B., 1964. Biochim. Biophys Acta 89: 189–190.

    Google Scholar 

  8. Andria, G. & Taniuchi, H., 1978. J. Biol. Chem. 253: 2262–2270.

    Google Scholar 

  9. Saxena, V. P. & Wetlaufer, D. B., 1970. Biochemistry 9: 5015–5022.

    Google Scholar 

  10. Hantgan, R. R., Hammes, G. G. & Scheraga, H. A., 1974. Biochemistry 13: 3421–3431.

    Google Scholar 

  11. Isemura, T., Takagi, T., Maeda, Y. & Imae, K., 1961. Biochem. Biophys. Res. Commun. 5: 373.

    Google Scholar 

  12. White, F. H., Jr., 1962. Fed. Proc., Fed. Am. Soc. Exp. Biol. 21: 233.

    Google Scholar 

  13. Epstein, C. J. & Goldberger, R. F., 1963. J. Biol. Chem. 238: 1380–1383.

    Google Scholar 

  14. Bradshaw, R. A., Kanarek, L. & Hill, R. L., 1967. J. Biol. Chem. 242: 3789–3798.

    Google Scholar 

  15. Yutani, K., Yutani, A., Imanishi, A., Isemura, T., 1968. J. Biochem. 64: 449–453.

    Google Scholar 

  16. White, F. H., 1976. Biochemistry 15: 2906.

    Google Scholar 

  17. Ristow, S. S. & Wetlaufer, D. B., 1973. Biochem. Biophys. Res. Commun. 50: 544–550.

    Google Scholar 

  18. Anderson, W. L. & Wetlaufer, D. B., 1976. J. Biol. Chem. 251: 3147.

    Google Scholar 

  19. Creighton, T. E., 1974. J. Mol. Biol. 87: 603–624.

    Google Scholar 

  20. Creighton, T. E., 1975. J. Mol. Biol. 95: 167–199.

    Google Scholar 

  21. Creighton, T. E., 1977. J. Mol. Biol. 113: 275–293.

    Google Scholar 

  22. Jocelyn, P. C., 1967. Eur. J. Biochem. 2: 327.

    Google Scholar 

  23. Jocelyn, P. C., 1972. Biochemistry of SH Groups. Academic Press, London.

    Google Scholar 

  24. Lapanje, S. & Rupley, J. A., 1973. Biochemistry 12: 2370.

    Google Scholar 

  25. Anfinsen, C. B., 1956. J. Biol. Chem. 221: 405–412.

    Google Scholar 

  26. Lin, M. C., 1970. J. Biol. Chem. 245: 6726–6731.

    Google Scholar 

  27. Taniuchi, H., 1970. J. Biol. Chem. 245: 5459–5468.

    Google Scholar 

  28. Haber, E. & Anfinsen, C. B., 1961. J. Biol. Chem. 236: 422–424.

    Google Scholar 

  29. Kato, I. & Anfinsen, C. B., 1969. J. Biol. Chem. 244: 1004.

    Google Scholar 

  30. Taniuchi, H., 1973. J. Biol. Chem. 248: 5164–5174.

    Google Scholar 

  31. Taniuchi, H. & Bohnert, 1975. J. Biol. Chem. 250: 2388–2394.

    Google Scholar 

  32. Taniuchi, H., Acharya, A. S., Andria, G. & Parker, D. S., 1977. Adv. Exper. Med. Biol. 86A: 51–66.

    Google Scholar 

  33. Creighton, T. E., 1977. J. Mol. Biol. 113: 329–341.

    Google Scholar 

  34. Garel, J. R., 1978. J. Mol. Biol. 118: 331–345.

    Google Scholar 

  35. Chavez, L. G., Jr. & Scheraga, H., 1980. Biochemistry 19: 1005–1012.

    Google Scholar 

  36. Sachs, D. H., Schechter, A. N., Eastlake, A. & Anfinsen, C. B., 1972. Proc. Natl. Acad. Sci. U.S.A. 60: 3790–3794.

    Google Scholar 

  37. Parker, D. S., Davis, A. & Taniuchi, H., 1981. J. Biol. Chem. 256: 4557–4569.

    Google Scholar 

  38. Acharya, A. S. & Taniuchi, H., 1976. J. Biol. Chem. 251: 6934–6946.

    Google Scholar 

  39. Acharya, A. S. & Taniuchi, H., 1977. Proc. Natl. Acad. Sci. U.S.A. 74: 2362–2366.

    Google Scholar 

  40. Acharya, A. S. & Taniuchi, H., 1978. Biochemistry 17: 3064–3070.

    Google Scholar 

  41. Acharya, A. S. & Taniuchi, H., 1980a. J. Biol. Chem. 255: 1905–1911.

    Google Scholar 

  42. Acharya, A. S. & Taniuchi, H., 1980b. Int. J. Pept. and Prot. Res. 15: 503–509.

    Google Scholar 

  43. Acharya, A. S. & Taniuchi, H., 1980c. Biophys. J. 32: 425–426.

    Google Scholar 

  44. Canfield, R. E., 1963., J. Biol. Chem. 238: 2698–2807.

    Google Scholar 

  45. Canfield, R. E. & Liu, A. K., 1965. J. Biol. Chem. 240: 1997–2002.

    Google Scholar 

  46. Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C. & Sarma, V. R., Nature 206: 757–761.

  47. Harrington, W. F. & Schellman, J. A., 1956. Cr. Trav. Lab. Carlsberg 30: 21.

    Google Scholar 

  48. Harrington, W. F. & Sela, M., 1959. Biochim. Biophys. Acta 31: 427–434.

    Google Scholar 

  49. Haber, E. & Anfinsen, C. B., 1962. J. Biol. Chem. 237: 1839–1844.

    Google Scholar 

  50. Andria, G. & Taniuchi, H., 1971. Fed. Proc. 30: 1288.

    Google Scholar 

  51. Habeeb, A. F. S. A., 1967. Arch. Biochem. Biophys. 121: 652–664.

    Google Scholar 

  52. Andrews, P., 1964. Biochem. J. 91: 222–233.

    Google Scholar 

  53. Light, A. & Sinha, N. K., 1976. Biochem. Biophys. Res. Commun. 68: 1188–1193.

    Google Scholar 

  54. Bewly, T. A. & Li, C. H., 1969. Int. J. Pept. Protein 1: 117–124.

    Google Scholar 

  55. Levinthal, C., 1968. J. Chim. Phys. 65: 44–45.

    Google Scholar 

  56. Tanford, C., 1968. Adv. Protein Chem. 23: 121–282.

    Google Scholar 

  57. Arnone, A., Bier, C. J., Cotton, F. A., Day, V. W., Hazen, E. E., Jr., Richardson, D. C., Richardson, J. & Yonuth, A., 1971. J. Biol. Chem. 246: 2302–2316.

    Google Scholar 

  58. Taniuchi, H. & Anfinsen, C. B., 1971. J. Biol. Chem. 246: 2291–2301.

    Google Scholar 

  59. Richards, F. M. & Vithayathil, P. J., 1959. J. Biol. Chem. 234: 1459.

    Google Scholar 

  60. Taniuchi, H., Anfinsen, C. B. & Sodja, A., 1967. Proc. Natl. Acad. Sci. U.S.A. 58: 1235–1242.

    Google Scholar 

  61. Perraudin, J. P., Oh-Johanson, K. J., Berga, S. E., Torchia, T., Voet, J. G., & Wetlaufer, D. B., 1978. Fed. Proc. 37: 1275.

    Google Scholar 

  62. Ottesen, M. & Stracker, A., 1960. C. R. Lab Carlsberg Ser. Chim. 34: 457–467.

    Google Scholar 

  63. Sela, M. & Anfinsen, C. B., 1957. Biochim. Biophys. Acta 24: 229–235.

    Google Scholar 

  64. Cuatrecasas, P., Taniuchi, H. & Anfinsen, C. B., 1968. Brookhaven Symp. in Biology 21: 172–200.

    Google Scholar 

  65. Cuatrecasas, P., Fuchs, S. & Anfinsen, C. B., 1967. J. Biol. Chem. 242: 3063.

    Google Scholar 

  66. Parr, G. R. & Taniuchi, H., 1980. J. Biol. Chem. 255: 2616–2623.

    Google Scholar 

  67. Kauzmann, W., 1959. Adv. Protein Chem. 14: 1–63.

    Google Scholar 

  68. Rosa, J. & Richards, F. M., 1981. J. Mol. Biol. 145: 835–851.

    Google Scholar 

  69. Wüthrich, K., Roder, H. & Wagner, G., 1979. In: Protein Folding (Jaenicke, R., ed.) Elsevier/North-Holland Biochemical Press, Amsterdam, pp. 549–562.

  70. Labhardt, A. & Baldwin, R. L., 1979. J. Mol. Biol. 135: 231–244.

    Google Scholar 

  71. Brandts, J. F., Halvorson, H. R. & Brennan, M., 1975. Biochemistry 14: 4953–4963.

    Google Scholar 

  72. Parr, G. R. & Taniuchi, H., 1979. J. Biol. Chem. 254: 4836–4842.

    Google Scholar 

  73. Karplus, M. & Weaver, D. L., 1976. Nature 260: 404–406.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Rockefeller University, New York, USA

    A. Seetharama Acharya

  2. Laboratory of Chemical Biology, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, National Institutes of Health, 20205, Bethesda, MD, USA

    Hiroshi Taniuchi

Authors
  1. A. Seetharama Acharya
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Hiroshi Taniuchi
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Acharya, A.S., Taniuchi, H. Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation. Mol Cell Biochem 44, 129–148 (1982). https://doi.org/10.1007/BF00238502

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00238502

Keywords

Search

Navigation