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Características del principio antidiurético liberado del suero sanguíneo por la acción de la pepsina /
Abstract
Tesis (Licenciatura en medicina)--Universidad de Chile, Facultad de Biología y Ciencias Médicas, 1951-1952.
In 1942 the uncertainty about the enzymatic character of renin promoted investigations to establish whether typical proteolytic enzymes, such as those elaborated by digestive glands, could reproduce the action of renin upon the same blood substrates. The first experiments [Croxatto and Croxatto, 1941 (2)] not only showed that pepsin reproduced the typical action of renin, giving rise to a peptide similar to angiotensin, but also opened a new exploratory technique that strengthened the view that blood proteins are a rich potential source of vasoactive peptides. In fact, the well-known proteolytic enzymes of the digestive tract can produce vasoactive peptides similar or identical to those released by endogenous enzymatic systems (renin, kallikrein). However, the activity of the latter enzymes is far more restricted. Renin acts exclusively upon renin-substrate or its synthetic homologue, but it does not liberate kinins from kininogens and, in contrast, plasma kallikreins are unable to produce angiotensin from blood substrates. On the other hand, endopeptidases such as pepsin, trypsin and chymotrypsin can hydrolyze both renin-substrate and kininogen. In the terminal products of the hydrolyzate, it is possible to characterize angiotensin- and bradykinin-like peptides among the other pharmacologically active substances which are less known.
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