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. 1979;23(6):633-40.
doi: 10.1002/food.19790230609.

[Spontaneous solubilization of mcuosal peptide hydrolases in rat small intestine]

[Article in German]

[Spontaneous solubilization of mcuosal peptide hydrolases in rat small intestine]

[Article in German]
R Mooz et al. Nahrung. 1979.

Abstract

In vitro incubations of small intestine preparation lead to the spontaneous release of mucosal enzymes into the incubation medium, due to superficial dissolution and membrane lesions. One-hour anaerobic incubation of everted small intestine segments produces the liberation of from 13% (leucine arylamidase) to 30% (Gly-L-Pro-splitting peptide hydrolase) of the mucosal enzyme activities. Under the conditions of in vivo perfusion, the solubilization rates are from 50 to 80% lower than these values. The tendency to solubilization is only in part reduced to a significant extent by the saturation of the incubation medium with oxygen, but it does not reach the in vivo level. The detectability of membrane-bound and intracellular marker enzymes in the incubation medium permits no conclusions concerning the physiological localization of the released peptidases.

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