Fidge N, Kagami A, O'Connor M
Biochem Biophys Res Commun. 1985 Jun 28;129(3):759-65. doi: 10.1016/0006-291x(85)91957-6.
A protein band with an apparent molecular weight of 78,000 daltons has been identified in the solubilised plasma membrane extract of sheep adrenal cortex which binds HDL3 devoid of E apolipoprotein. Following 'Western' blotting, and development of the nitrocellulose strips with appropriate antisera and color reagent, the same band, unlike other cortical membrane proteins or albumin, bound AI and AII apolipoproteins. Human LDL bound weakly to the same band but more strongly to another two proteins of higher molecular weight. These studies confirm the same degree of specificity of HDL3 binding found with cultured adrenal cells and strengthen the suggested existence of a specific HDL receptor.
在绵羊肾上腺皮质的可溶性质膜提取物中,已鉴定出一条表观分子量为78,000道尔顿的蛋白带,它能结合不含E载脂蛋白的HDL3。经过“Western”印迹法,并用适当的抗血清和显色试剂处理硝酸纤维素条带后,与其他皮质膜蛋白或白蛋白不同,同一条带能结合AI和AII载脂蛋白。人低密度脂蛋白与同一条带的结合较弱,但与另外两种分子量较高的蛋白结合更强。这些研究证实了在培养的肾上腺细胞中发现的HDL3结合的相同特异性程度,并进一步证明了特定HDL受体的存在。