大鼠肾髓质间质细胞中的B2缓激肽受体样结合

B2 bradykinin receptor-like binding in rat renomedullary interstitial cells.

作者信息

Fredrick M J, Abel F C, Rightsel W A, Muirhead E E, Odya C E

出版信息

Life Sci. 1985 Jul 29;37(4):331-8. doi: 10.1016/0024-3205(85)90503-x.

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.

摘要

制备了来自培养大鼠肾髓质间质细胞（RRIC）的微粒部分用于缓激肽（BK）结合研究。将三种放射性标记的BK类似物，即[125I-Tyr1]胰激肽、[125I-Tyr5]-BK和[125I-Tyr8]-BK与微粒部分一起孵育，导致这些肽发生降解。确定了防止这些放射性标记激肽水解的测定条件。在这些条件下，以[125I-Tyr1]胰激肽（TlK）作为放射性配体进行了直接结合研究。BK的结合亲和力，表观缔合常数Kassoc. = 1.3×10(9) M-1，以及用51种BK类似物确定的特异性，与B2 BK受体所预期的一致。