saralasin and 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

125I-labelled angiotensin II (A II) specifically binds to solubilized receptors extracted from rat isolated glomeruli using CHAPS (3-[3-( cholamidopropyl ) dimethylammonio ]-1-propanesulfonate). The yield of solubilization of the binding sites was 3.3%. Equilibrium was reached after 15-20 min and specific binding represented 75% of total binding. Dissociation of the hormone-receptor complex after addition of an excess of A II was very slow in the presence of Ca2+ and Mg2+. [Sar1 Ala8] A II and [Sar1 Ile8] A II were more potent as competitive inhibitors of 125I-labelled A II than A II itself and its heptapeptide. These basic features of 125I-labelled A II binding to the extracted material were similar to those observed previously with untreated glomeruli.

Topics: 1-Sarcosine-8-Isoleucine Angiotensin II; Angiotensin II; Animals; Binding, Competitive; Cholic Acids; Detergents; Kidney Glomerulus; Male; Rats; Rats, Inbred Strains; Receptors, Angiotensin; Receptors, Cell Surface; Saralasin; Solubility