Affiliation:
1. From the Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J.
Abstract
A protein fraction has been isolated from crude pepsin preparations which is about 400 times as active as crystalline pepsin in the lique-faction of gelatin.
The activity as measured by the digestion of casein, edestin or egg albumin is less than that of crystalline pepsin.
It is more resistant to alkali than the crystalline pepsin.
Publisher
Rockefeller University Press
Cited by
34 articles.
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3. Pepsin B;Handbook of Proteolytic Enzymes;2004
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5. Purification of human gastric proteases by immunoadsorbents;Biochimica et Biophysica Acta (BBA) - Protein Structure;1976-04