Inhibition of enzymatic degradation of angiotensin II in membrane binding assays: utility of 1,10-phenanthroline.
Studies of 125I-labelled angiotensin II binding to membranes from bovine uterus and aorta are rendered impossible because enzymatic degradation of 90% of the added ligand occurs within 30 min at 23 degrees C. High pressure liquid chromatographic analysis has demonstrated that a single iodinated product, which is more hydrophilic than intact angiotensin II, is produced by enzymatic cleavage. Investigation of a series of enzyme inhibitors has shown that the carboxypeptidase inhibitor 1,10-phenanthroline completely inhibits degradation of angiotensin II without disrupting ligand binding.
Koziarz
P
P
Department of Medical Biochemistry, University of Calgary, Alta., Canada.
Moore
G J
GJ
D000804:Angiotensin II / Q000378:metabolism*; D000818:Animals; D001013:Aorta, Thoracic / Q000378:metabolism; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004492:Edetic Acid / Q000494:pharmacology; D005260:Female; D066298:In Vitro Techniques; D010618:Phenanthrolines / Q000494:pharmacology*; D011869:Radioligand Assay; D014599:Uterus / Q000378:metabolism
D010618:Phenanthrolines; D000804:Angiotensin II; D004492:Edetic Acid; D002268:Carboxypeptidases; C025205:1,10-phenanthroline