Letter | Published:

Sedimentation of β-Lactoglobulin (A,B) under Dissociating Conditions in Acid Solution

Naturevolume 192page1181 (1961) | Download Citation

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Abstract

EVIDENCE that β-lactoglobulin molecules dissociate into halves in the pH region 1.6–4 has been presented by Timasheff, Townend and Weinberger1–3, and they have shown3 that there is reasonable agreement between the results obtained by the complementary methods of ultracentrifugation and light-scattering. The overall picture which emerges is of a dumb-bellshaped4 lactoglobulin molecule, of axial ratio 2, dissociating reversibly at 25° below pH 4 into two spherical sub-units of equal size. According to light-scattering data, and on the assumption of a molecule of weight 36,000, the dissociation constant at pH 1.6 is 2.5 × 10−4 mol./l. and at pH 3.5 is 4.3 × 10−6 mol./l.3.

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References

  1. 1

    Townend, R., and Timasheff, S. N., J. Amer. Chem. Soc., 79, 3613 (1957).

  2. 2

    Timasheff, S. N., and Townend, R., J. Amer. Chem. Soc., 83, 470 (1961).

  3. 3

    Townend, R., Weinberger, L., and Timasheff, S. N., J. Amer. Chem. Soc., 82, 3175 (1960).

  4. 4

    Green, D. W., and Aschaffenburg, R., J. Mol. Biol., 1, 54 (1959).

  5. 5

    Gilbert, G. A., Nature, 186, 882 (1960).

  6. 6

    Perrin, F., J. Phys. Radium, 7, 1 (1936).

  7. 7

    Svedberg, T., and Pedersen, K., The Ultracentrifuge, 28 (Oxford University Press, London, 1940).

  8. 8

    Gilbert, G. A., Proc. Roy. Soc., A, 250, 377 (1959).

  9. 9

    Gilbert, G. A., Abst. Intern. Biophys. Cong. Stockholm, 312 (1961).

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Affiliations

  1. Department of Chemistry, The University, Birmingham, 15

    • LILO M. GILBERT
    •  & G. A. GILBERT

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https://doi.org/10.1038/1921181a0

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