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A correction to this article has been published: J. Gen. Physiol. 14 (5) 683
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The Journal of General Physiology, Vol 13, 739-766, Copyright © 1930 by The Rockefeller University Press

ARTICLE

CRYSTALLINE PEPSIN

I. ISOLATION AND TESTS OF PURITY



John H. Northrop 1

1 From the Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J.

A method is described for the preparation of a crystalline protein from commercial pepsin preparations which has powerful peptic activity. The composition, optical activity, and proteolytic activity of this protein remain constant through seven successive crystallizations. No evidence for the presence of a mixture or of a solid solution is found in a study of the solubility of the protein in a series of different salt solutions, nor from the diffusion coefficient or from the rate of inactivation. These results indicate that the material is a pure substance or possibly a solid solution of two or more substances having nearly the same solubility in all the various solvents studied. It seems reasonable to conclude from these experiments that the possibility of a mixture must be limited to a mixture of proteins, so that the conclusion seems justified that pepsin itself is a protein.

Accepted on May 9, 1930


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