Die milchkoagulierenden Enzyme der Magenschleimhaut und ihre Zymogene.

Abstract

Pepsinogen differs from prorennin in that the former can clot milk. The pH of activation is different for each. At pH 2.8 prorennin is fully activated, whereas pepsinogen at 7.5 to 2.8 can not attack protein or clot milk. Pepsinogen needs a much higher H-ion cone. (pH 1.0). Ethyl alcohol destroys pepsinogen but not pepsin. The mucosa of the adult animal does not contain prorennin (rennin zymo-gen) but only inactive pepsinogen. Pepsinogen may be prepared in an inactive dry form and activated by HC1. Contrary to earlier findings it is shown that pepsin also can act as a milk-clotting enzyme.