Premium
THE ACTION OF TRYPSIN AND OF CHYMOTRYPSIN ON PHENYLTHIOCARBAMYL‐ANGIOTENSIN II
Author(s) -
Osborn EC,
Doyle AE,
Murray M
Publication year - 1967
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1967.21
Subject(s) - trypsin , chymotrypsin , angiotensin ii , chemistry , arginine , valine , renin–angiotensin system , angiotensin iii , asparagine , biochemistry , angiotensin receptor , endocrinology , enzyme , amino acid , biology , receptor , blood pressure
Summary The effects of incubaling angiotensin II (valyl 5 ‐angiotensin II‐ aspartic‐ β ‐amide) and a mixture of [ 35 S] and [ 32 S] phenylthiocarbainyl‐angiotensin II (PTC‐angiotensin) with trypsin and chymotrypsin at varying concentrations have been studied, and the chromatographic and electrophoretic properties of the breakdown products determined The results indicate that PTC‐angiotensin, like angiotensin, is readily split by trypsin between arginine and valine 3 and by chymotrypsin between tyrosine and valine. The rate of destruction by the two enzymes, as judged by the decline in pressor activity, was similar with both compounds. In addition to the expected cleavage between arginie and valine 3 , trypsin induced cleavage between asparagine and arginine, in PTC‐angiotensin but not in angiotensin, with the liberation of free arginine and PTC‐asparagine.