THE PRESENCE OF A GELATIN-LIQUEFYING ENZYME IN CRUDE PEPSIN PREPARATIONS

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 a...

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Detalles Bibliográficos
Autor principal: Northrop, John H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1931
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141139/
https://www.ncbi.nlm.nih.gov/pubmed/19872625
Descripción
Sumario: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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