Abstract
CRYSTALLIZED pepsin has been shown by Tiselius et al.1 to give one sharp and a second, diffuse, boundary, visible at higher concentrations only. During electrophoresis, inactive material was removed and the specific activity of the pepsin was raised by 31–69 per cent. These authors concluded that the homogeneity of the migration of the active component is not sufficient evidence per se for the chemical individuality of the enzyme. Solubility studies revealed several components possessing different activities (refs. in Sumner and Somers2).
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References
Tiselius, A., Henschen, G. E., and Svensson, H., Biochem. J., 32, 1814 (1938).
Sumner, J. B., and Somers, G. F., “Chemistry and Methods of Enzymes” (Academic Press, Inc., New York, 1947).
Hoch-Ligeti, C., and Hoch, H., Biochem. J., 43, 556 (1948).
Svensson, H., Ark. Kem. Min. Geol., 22, No. 10 (1946).
Dole, V. P., J. Amer. Chem. Soc., 67, 1119 (1945).
Hoch, H., Biochem. J., 42, 181 (1948).
Anson, M. L., J. Gen. Physiol., 22, 79 (1938).
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HOCH, H. Electrophoretic Heterogeneity of Crystallized Pepsin. Nature 165, 278–279 (1950). https://doi.org/10.1038/165278a0
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DOI: https://doi.org/10.1038/165278a0
