Letter | Published:

Liberation of Tyrosine Hydroxyl Groups in Urea Solutions of Bovine Serum Albumin and Ovalbumin

Naturevolume 180pages12861287 (1957) | Download Citation



THE process of denaturation of proteins is being investigated in this laboratory by following changes in various properties which depend on the structure and the state of aggregation of the protein molecule1. In view of the possible importance of hydrogen-bonded tyrosine hydroxyl groups in maintaining the native configuration of the protein molecule2 the liberation of tyrosine hydroxyl groups has been studied by examining the changes with time in the ultra-violet absorption spectra of bovine serum albumin and ovalbumin under different conditions of pH, both in the presence and absence of urea.

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    McKenzie, H. A., Smith, M. B., and Wake, R. G., Nature, 176, 738 (1955).

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    Beaven, G. H., and Holiday, E. R., “Adv. Protein Chem.”, 7, 319 (1952).

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    Laskowski, jun., M., Widom, J. M., McFadden, M. L., and Scheraga, H. A., Biochim. Biophys. Acta, 19, 583 (1956).

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    Tanford, C., Buzzell, J. G., Rands, D. G., and Swanson, S. A., J. Amer. Chem. Soc., 77, 6421 (1955).

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    Harrington, W. F., Biochim. Biophys. Acta, 18, 450 (1955).

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    Simpson, R. B., and Kauzmann, W., J. Amer. Chem. Soc., 75, 5139 (1953).

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  1. C.S.I.R.O. Division of Food Preservation, Physico-Chemical Unit and the Biochemistry Department, University of Sydney

    • A. N. GLAZER
    • , H. A. McKENZIE
    •  & R. G. WAKE


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