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.
Similar content being viewed by others
Article PDF
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).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
PERLMANN, G. Formation of Enzymatically Active, Dialysable Fragments during Autodigestion of Pepsin. Nature 173, 406 (1954). https://doi.org/10.1038/173406a0
Issue Date:
DOI: https://doi.org/10.1038/173406a0
This article is cited by
-
Aminos�ure-Sequenzen in Proteinen
Die Naturwissenschaften (1959)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.