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Effect of Ionizing Radiation on Protein Denaturation

Naturevolume 169pages965966 (1952) | Download Citation



IT has long been known that the stability of proteins with respect to denaturation (as defined by aggregation) is lowered upon treatment with ionizing radiation1. Detailed studies are lacking, however. We have found that the denaturation of solutions of egg albumin and hæmoglobin subjected to X-rays (the denaturation kinetics of which in the intact state is known2) can be defined quantitatively by the usual coagulation method, its validity being established by order of reaction studies on dilutions of the complex irradiated systems. By this procedure it was found that the heterogeneous protein material of these systems was (at ordinary pH) initially undenatured and contained relatively large quantities of species of decreased thermal stability, characterized by much reduced values of both the Arrhenius frequency factor (ν) and the energy of activation (E) of their first-order denaturation velocity-constants.

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    Fernau, A., and Pauli, W., Biochem. Z., 70, 426 (1915). Wels, P., Pflügers Arch., 199, 226 (1923). Fernau, A., and Spiegel-Adolf, M., Biochem. Z., 204, 14 (1929). Arnow, L. E., J. Biol. Chem., 110, 43 (1935).

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    Chick, H., and Martin, E., Kolloidchem. Beihefte, 5, 49 (1914). Lewis, P. S., Biochem. J., 20, 965 (1926).

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    Svedberg, T., and Brohult, S., Nature, 143, 938 (1939).

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    Anderson, R. S., Fed. Proc., 9, 6 (1950). Kaufmann, B. P., McDonald, M. R., and Gay, H., Year Book, Carnegie Inst. Wash., 49, 173 (1949–50).

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  1. Biological Laboratory, Cold Spring Harbor, N.Y.



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