Abstract
Hypertensin (angiotonin) and pepsitensin were inactivated by an aminopeptidase (a. p.) enzyme from yeast in a few mins. incubation at 38[degree] and neutral pH. The Loewen Trendelenburg test and arterial pressure of the cat were used as methods of determining degree of destruction. Hypertensinase extracts of pig kidneys and aminopeptidase hydrolyzed l-leucylglycine. the former hydrolyzed dl-methyl leucyldiglycine but aminopeptidase had no action. The effect of aminopeptidase on hypertensin and pepsitensin confirmed their polypeptid nature and strengthened the supposition that they possessed a free NH2 radical.