The ability of gastric juice to clot milk has been ascribed by Hammarsten to a special proteolytic enzyme, chymosin or rennin. The Pavlov school and others, however, have long maintained that there is no necessity of attributing rennet action to a special organic catalyst. This view was seemingly supported by the well known fact that practically all proteolytic enzymes, even those from vegetable sources such as papain from the melon tree, can effect the clotting of milk. In his last contribution to this subject, in 1923, Hammarsten concluded that there was no positive proof against identity of pepsin and rennin.
Recently Kleiner and Tauber1 have reported the isolation, in comparatively pure form, of a rennin preparation from the mucosa of the fourth stomach of the calf. This preparation shows the highest clotting power yet reported; at the same time it is practically devoid of peptic activity. The elementary composition
PEPSIN AND RENNIN. JAMA. 1932;99(10):835–836. doi:10.1001/jama.1932.02740620045014
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