Über Aminopolypeptidase. (II. Mitteilung.)

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Abstract
The activation of purified amino-polypeptidases from the intestine of the pig was investigated. P was eliminated by dialysis. Below a certain amount of P, there was proportionality between P-content and enzyme activity. Dialysis against M/200 phosphate did not inactivate the peptidase. A chemical linkage of phosphate with the enzyme is not considered probable, for though the ratio, phosphorus content/activity, was constant, this constancy was not the same in different enzyme preparations. A simple adsorption could not be postulated, as inactivated preparations could not be activated by phosphate or pyrophosphate, though dialysis liquor contained an activating substance. It is possible that P forms an integral component of an activating system: The partial inactivation of the enzyme had no influence upon the specificity. It seems improbable, therefore, that the enzyme is a complex one, the more so as preparations purified with different adsorbents (Fe-hydroxide and Fe-phosphate) had the same affinity for the same substrate.

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