Characterization of the glucagon receptor and its functional domains using monoclonal antibodies.
作者： V Iwanij , A C Vincent
DOI: 10.1016/S0021-9258(17)45360-9
关键词:
摘要: Four monoclonal antibodies, designated 4H11, 6E10, 2C5, and 3E9 were prepared against partially purified rat hepatic glucagon receptor. These antibodies characterized by their ability to recognize the receptor in target tissues using immunoblot immunoprecipitation procedures. The recognized a 62-kDa band liver, kidney, adipose tissue but not lung, adrenals, erythrocytes, indicating high degree of specificity. different antigenic determinants; 6E10 2C5 bind protein epitopes, while 4H11 carbohydrate epitopes. Furthermore, proteolytic mapping established that domains molecule. used study immunochemical similarities among receptors from species assess topological location ligand-binding site. By combining techniques affinity cross-linking, mapping, antibody binding, we have identified glucagon-binding site near COOH-terminal domain
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