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B2 bradykinin receptor-like binding in rat renomedullary interstitial cells

Journal Article · · Life Sci.; (United States)

A particulate fraction from cultured rat renomedullary interstitial cells (RRIC) was prepared for bradykinin (BK) binding studies. Incubation of three radiolabeled BK analogs, (/sup 125/I-Tyr/sup 1/)kallidin, (/sup 125/I-Tyr/sup 5/)-BK, and (/sup 125/I-Tyr/sup 8/)-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 (/sup 125/I-Tyr/sup 1/)kallidin (T1K) as the radioligand. BK binding affinity, apparent K/sub assoc/ = 1.3 x 10/sup 9/ M/sup -1/, and specificity, determined with 51 BK analogs, were consistent with those expected of a B2 BK receptor. 17 references, 2 figures, 2 tables.

Research Organization:
Indiana Univ., Bloomington
OSTI ID:
5411389
Journal Information:
Life Sci.; (United States), Journal Name: Life Sci.; (United States) Vol. 37:4; ISSN LIFSA
Country of Publication:
United States
Language:
English