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Behavior of S1- and S2-Ovalbumin and S-Ovalbumin A1 in Urea Solution: Kinetics and Equilibria

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Abstract

The isolation of S-, S1-, and S2-ovalbumin from domestic hen egg R-ovalbumin and of two methods for S-ovalbumin A1 are described. The first is by heat treatment of R-ovalbumin A1 and the second is of R-ovalbumin followed by fractionation on Sepharose. A kinetics and equilibrium study is made of their behavior in the presence of urea and compared with that of R-ovalbumins. As anticipated, the S-ovalbumins are much more resistant to urea than R-ovalbumins. Unlike the latter, S-ovalbumins' equilibrium profiles have a simpler sigmoidal shape. The unfolding of S1- and S2-ovalbumin is an order of magnitude slower than that of R-ovalbumin. Some possible structural differences between R- and S-ovalbumin forms and their significance are discussed.

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Authors and Affiliations

  1. School of Chemistry, University College, University of New South Wales, Australian Defence Force Academy, Canberra, Australia, 2600

    Hugh A. McKenzie

  2. John Curtin School of Medical Research, Australian National University, GPO Box 334, Canberra, Australia, 2601

    Robert D. Frier

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  1. Hugh A. McKenzie
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  2. Robert D. Frier
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Correspondence to Hugh A. McKenzie.

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Deceased December 8, 2001

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McKenzie, H.A., Frier, R.D. Behavior of S1- and S2-Ovalbumin and S-Ovalbumin A1 in Urea Solution: Kinetics and Equilibria. J Protein Chem 22, 215–220 (2003). https://doi.org/10.1023/A:1025028705586

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