The study characterizes specific high-affinity binding sites for angiotensin II in rat renal epithelial cell membranes, providing basic science insights into angiotensin receptor pharmacology.
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Requires human validation before clinical consideration; extends preclinical angiotensin II receptor characterization.
1 Specific high affinity binding sites for [125I]-angiotensin II have been identified in crude basolateral and brush border membranes from rat cortex. 2 A central high affinity site, KD 0.62 nM; Bmax 299 fmol/mg was identified as part of a complex multicomponent binding system. 3 This high affinity site was saturable and exhibited specificity for angiotensin II analogues and closely related peptides but not for bradykinin, substance P or peptide fragments of angiotensin II. 4 Specific [125I]-angiotensin II binding was partially dependent on NaCl. Absence of NaCl resulted in a decrease in Bmax, had no effect on the rate of association but increased the rate of dissociation of [125I]-angiotensin from its binding site.
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Cox et al. (1983) studied this question.
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