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The binding of [125I]‐angiotensin to rat renal epithelial cell membranes

journal contribution
posted on 1983-01-01, 00:00 authored by Helen CoxHelen Cox, K A Munday, J A Poat
Specific high affinity binding sites for [125I]‐angiotensin II have been identified in crude basolateral and brush border membranes from rat renal cortex. A central high affinity site, KD 0.62 nM; Bmax 299 fmol/mg was identified as part of a complex multicomponent binding system. 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. 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. 1983 British Pharmacological Society

History

Journal

British Journal of Pharmacology

Volume

79

Issue

1

Pagination

63 - 70

ISSN

0007-1188

eISSN

1476-5381

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