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.
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Copyright, 1931, by The Rockefeller Institute for Medical Research
1931
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