B2 bradykinin receptor-like binding in rat renomedullary interstitial cells |
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Authors: | M J Fredrick F C Abel W A Rightsel E E Muirhead C E Odya |
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Affiliation: | 1. Indiana University School of Medicine, Medical Sciences Program, Bloomington, IN 47405 USA |
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Abstract: | A particulate fraction from cultured rat renomedullary interstitial cells (RRIC) was prepared for bradykinin (BK) binding studies. Incubation of three radiolabeled BK analogs, [125I-Tyr1]kallidin, [125I-Tyr5]-BK, and [125I-Tyr8]-BK, with the particulate fraction resulted in degradation of these peptides. Assay conditions which prevented hydrolysis of these radiolabeled kinins were determined. Under these conditions, direct binding studies were performed with [125I-Tyr1]kallidin (TlK) as the radioligand. BK binding affinity, apparent Kassoc. = 1.3 X 10(9) M-1, and specificity, determined with 51 BK analogs, were consistent with those expected of a B2 BK receptor. |
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Keywords: | To whom correspondence should be addressed |
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