B2 bradykinin receptor-like binding in rat renomedullary interstitial cells
1985; Elsevier BV; Volume: 37; Issue: 4 Linguagem: Inglês
10.1016/0024-3205(85)90503-x
ISSN1879-0631
AutoresMark J. Fredrick, Fred C. Abel, Wilton A. Rightsel, E. E. Muirhead, Charles E. Odya,
Tópico(s)Renin-Angiotensin System Studies
ResumoA 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 (T1K) as the radioligand. BK binding affinity, apparent Kassoc. = 1.3 × 109 M−1, and specificity, determined with 51 BK analogs, were consistent with those expected of a B2 BK receptor.
Referência(s)