Reynolds J A
Biochemistry. 1984 Mar 13;23(6):1124-9. doi: 10.1021/bi00301a014.
Apolipoprotein AI from human serum high-density lipoprotein has been recombined with egg yolk lecithin from ternary complexes of detergent-lipid-protein to from homogeneous spherical particles with maximum binding of 220 mol of lipid/2 mol of AI. This complex differs from those formed when n-alkyl detergents or short chain saturated diacylphosphatidylcholines interact with AI in that the maximum hydrophobic volume accommodated by the protein is increased as the result of increased alpha-helix content. Additionally, it is shown that no interaction occurs between AI and didecanolyphosphatidylcholine or egg yolk lecithin above their thermotropic phase transitions and in the absence of single-tail amphiphiles.
人血清高密度脂蛋白中的载脂蛋白AI已与去污剂-脂质-蛋白质三元复合物中的蛋黄卵磷脂重组,形成均匀的球形颗粒,最大结合量为220摩尔脂质/2摩尔AI。该复合物与正烷基去污剂或短链饱和二酰基磷脂酰胆碱与AI相互作用时形成的复合物不同,因为蛋白质容纳的最大疏水体积因α-螺旋含量增加而增大。此外,研究表明,在高于热致相变温度且不存在单尾两亲物的情况下,AI与二癸酰磷脂酰胆碱或蛋黄卵磷脂之间不发生相互作用。