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Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution

Nature volume 176, page 738 (1955)Cite this article

Abstract

SINCE 1902, when Ramsden1 described the effects of urea on “proteids”, there has been much speculation regarding the molecular weights of proteins in urea solution. Some workers have claimed that aggregation does not take place in the urea denaturation of ovalbumin and bovine serum albumin. In spite of this, it is well known that their urea solutions frequently form gels when the protein concentration is high. Recently, Kauzmann et al. 2,3 have studied the viscosity changes accompanying the urea denaturation of these proteins and the gelling time for ovalbumin. Under certain conditions an aggregation dependent upon concentration occurred, and this was interpreted in terms of hydrogen bonding and inter-molecular disulphide bonds (the latter through the —SS— and —SH exchange reaction of Huggins, Tapley and Jensen4).

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References

  1. Ramsden, W., J. Physiol., 28, xxiii (1902).

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  2. Frensdorff, H. K., Watson, M. T., and Kauzmann, W., J. Amer. Chem. Soc., 75, 5157, 5167 (1953).

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  3. Kauzmann, W., “The Mechanism of Enzyme Action”, 70 et seq. (edit. W. D. McElroy and B. Glass) (Johns Hopkins, Baltimore, 1954).

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  4. Huggins, C., Tapley, D. F., and Jensen, E. V., Nature, 167, 592 (1951).

    Article  ADS  CAS  Google Scholar 

  5. Edsall, J. T., “The Proteins” (edit. H. Neurath and K. Bailey), 1B, Chap. 7 (Academic Press, New York, 1953).

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Authors and Affiliations

  1. Commonwealth Scientific and Industrial Research Organization, Physico-Chemical Laboratory, Biochemistry Department, University of Sydney,

    H. A. McKENZIE, M. B. SMITH & R. G. WAKE

Authors
  1. H. A. McKENZIE
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  2. M. B. SMITH
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  3. R. G. WAKE
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McKENZIE, H., SMITH, M. & WAKE, R. Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution. Nature 176, 738 (1955). https://doi.org/10.1038/176738a0

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