Destruction of Hypertensin and Pepsitensin by an Aminopeptidase Obtained from Yeast
- 4 December 1942
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 96 (2501) , 519-520
- https://doi.org/10.1126/science.96.2501.519
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.This publication has 3 references indexed in Scilit:
- "Pepsitensin"—A Hypertensinlike Substance Produced by Peptic Digestion of ProteinsScience, 1942
- ON THE PROTEOLYTIC ENZYMES OF ANIMAL TISSUESJournal of Biological Chemistry, 1941
- ISOLATION AND PROPERTIES OF A PURE YEAST POLYPEPTIDASEPublished by Elsevier ,1941