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The binding of [ 125 I]‐angiotensin to rat renal epithelial cell membranes
Author(s) -
Cox Helen M.,
Munday Kenneth A.,
Poat Judith A.
Publication year - 1983
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1983.tb10496.x
Subject(s) - angiotensin ii , bradykinin , membrane , angiotensin iii , binding site , chemistry , renin–angiotensin system , brush border , renal cortex , peptide , angiotensin receptor , receptor , medicine , biochemistry , endocrinology , biophysics , biology , kidney , vesicle , blood pressure
1 Specific high affinity binding sites for [ 125 I]‐angiotensin II have been identified in crude basolateral and brush border membranes from rat renal cortex. 2 A central high affinity site, K D 0.62 n M ; B max 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 [ 125 I]‐angiotensin II binding was partially dependent on NaCl. Absence of NaCl resulted in a decrease in B max , had no effect on the rate of association but increased the rate of dissociation of [ 125 I]‐angiotensin from its binding site.