Abstract
NORTHROP and co-workers have shown1 that pepsin in solution digests itself with the formation of material soluble in trichloroacetic acid. The amount of non-protein substance formed depends upon factors such as time, temperature, and the pH and composition of the solvent. It has now been found in this laboratory that if autodigestion of pepsin proceeds at pH values removed from those optimal for proteolysis, pH 1.5–2.0, activity can be recovered in the non-protein fraction.
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References
Herriott, R. M., Desreux, V., and Northrop, J. H., J. Gen. Physiol., 24, 213 (1940).
Northrop, J. H., Kunitz, M., and Herriott, R. M., in “Crystalline Enzymes”, 74 and 81 (2nd edit., Columbia University Press, New York).
Baker, L. E., J. Biol. Chem., 193, 809 (1951).
Fruton, J. S., and Bergmann, M., J. Biol. Chem., 127, 627 (1939).
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PERLMANN, G. Formation of Enzymatically Active, Dialysable Fragments during Autodigestion of Pepsin. Nature 173, 406 (1954). https://doi.org/10.1038/173406a0
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DOI: https://doi.org/10.1038/173406a0
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