Jürss R, Hekman M, Helmreich E J
Biochemistry. 1985 Jun 18;24(13):3349-54. doi: 10.1021/bi00334a041.
A protease that can be inhibited by glutathione, dithiothreitol, and o-phenanthroline but not by ethylenediaminetetraacetic acid converts the 50-kilodalton beta-adrenergic receptor in turkey erythrocyte membranes to a 40-kDa polypeptide which retains the specific ligand binding site. This conversion is attenuated in intact erythrocytes. The large 50-kDa peptide contains N-linked, complex carbohydrates and is retained on wheat germ agglutinin-Sepharose. The 40-kDa product of proteolysis does not bind to the wheat germ agglutinin and can thus be separated from the 50-kDa polypeptide by lectin chromatography. However, the large difference in molecular weights of the two receptor peptides cannot be accounted for solely by the different extent of glycosylation.
一种可被谷胱甘肽、二硫苏糖醇和邻菲罗啉抑制，但不能被乙二胺四乙酸抑制的蛋白酶，将火鸡红细胞膜中的50千道尔顿β-肾上腺素能受体转化为一种40千道尔顿的多肽，该多肽保留了特定的配体结合位点。这种转化在完整的红细胞中会减弱。较大的50千道尔顿肽含有N-连接的复合碳水化合物，并保留在麦胚凝集素-琼脂糖上。蛋白水解产生的40千道尔顿产物不与麦胚凝集素结合，因此可通过凝集素色谱法与50千道尔顿多肽分离。然而，两种受体肽分子量的巨大差异不能仅由糖基化程度的不同来解释。
