Hypertensinase Activity of an L-Aminoacid Oxidase Preparation and of the Venom of Bothrops neuwidii

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Abstract
The hypertensinase activity of the l-amino acid oxidase prepn. of Blanchard et al. [see B. A. 19(2): entry 2257] was due to another enzyme present as an impurity. This was shown by the fact that the hypertensinase activity was not affected by absence of O2 or presence of ammonium sulfate. Furthermore the effect of pH on the hypertensinase activity was different from that shown for oxidase activity. Results obtained with a hypertensinase prepn. from the venom of Bothrops neuwidii supported the view that a proteolytic agent and not the l-amino acid oxidase was responsible for the inactivation of hypertensin.

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