Cervantes-Olivier P, Durieu-Trautmann O, Delavier-Klutchko C, Strosberg A D
Biochemistry. 1985 Jul 2;24(14):3765-70. doi: 10.1021/bi00335a052.
The turkey erythrocyte beta 1-adrenergic receptor can be purified by affinity chromatography on alprenolol-Sepharose and characterized by photoaffinity labeling with N-(p-azido-m-[125I]iodobenzyl)-carazolol. Through the use of the specific glycosidases neuraminidase and endo-beta-N-acetylglucosaminidase H and affinity chromatography on lectin-Sepharose gels, we show here that the receptor is an N-glycosyl protein that contains complex carbohydrate chains. No high-mannose carbohydrate chains appear to be present. The binding of the radiolabeled antagonist dihydroalprenolol to the receptor is affected neither by the enzymic treatments nor by the presence of lectins, suggesting that the carbohydrate moiety is not involved in the catecholamine binding site.
火鸡红细胞β1 - 肾上腺素能受体可用阿普洛尔 - 琼脂糖亲和层析法纯化，并用N -（对 - 叠氮 - 间 - [125I]碘苄基） - 咔唑洛尔进行光亲和标记来表征。通过使用特异性糖苷酶神经氨酸酶和内切β - N - 乙酰葡糖胺糖苷酶H以及在凝集素 - 琼脂糖凝胶上进行亲和层析，我们在此表明该受体是一种N - 糖基化蛋白，含有复杂的碳水化合物链。似乎不存在高甘露糖碳水化合物链。放射性标记的拮抗剂二氢阿普洛尔与该受体的结合既不受酶处理的影响，也不受凝集素存在的影响，这表明碳水化合物部分不参与儿茶酚胺结合位点。
