Krebs A, Fannon A, Racey T J, Rochon P, Depew W T, Singer M A
Biochem Cell Biol. 1987 Jan;65(1):56-61. doi: 10.1139/o87-008.
The hepatocyte membrane asialoglycoprotein receptor (ASGP-R) was extracted from rabbit liver, purified, and then incubated with preformed vesicles of dimyristoyl phosphatidylcholine. The association of protein with lipid was dependent on vesicle size and the best results were achieved with small vesicles of about 20 nm diameter. The ligand binding capacity of ASGP-R-vesicle complexes was also measured and found to be approximately sevenfold greater than free receptor in aqueous buffer and twofold greater than receptor solubilized in Triton X-100. Most likely, the reconstitution procedure used in these experiments does not result in transmembrane insertion of the receptor. ASGP-R probably resides on the surface of the vesicle, held there primarily by weak hydrophobic forces.
从兔肝脏中提取、纯化肝细胞膜去唾液酸糖蛋白受体（ASGP-R），然后将其与预先形成的二肉豆蔻酰磷脂酰胆碱囊泡一起孵育。蛋白质与脂质的结合取决于囊泡大小，直径约20 nm的小囊泡能取得最佳结果。还测量了ASGP-R-囊泡复合物的配体结合能力，发现其在水性缓冲液中的配体结合能力比游离受体大约高7倍，比溶解在Triton X-100中的受体高2倍。很可能这些实验中使用的重组程序不会导致受体跨膜插入。ASGP-R可能位于囊泡表面，主要通过弱疏水作用力固定在那里。
