The binding of [125I]-angiotensin to rat renal epithelial cell membranes.
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.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000804:Angiotensin II / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004848:Epithelium / Q000378:metabolism; D007668:Kidney / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D008871:Microvilli / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D011945:Receptors, Angiotensin / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism
D011945:Receptors, Angiotensin; D000804:Angiotensin II; D000469:Alkaline Phosphatase; D000254:Sodium-Potassium-Exchanging ATPase