STRUCTURE OF HUMAN-SERUM LIPOPROTEINS INFERRED FROM COMPOSITIONAL ANALYSIS

STRUCTURE OF HUMAN-SERUM LIPOPROTEINS INFERRED FROM COMPOSITIONAL ANALYSIS
复制标题

DOI:
10.1073/pnas.74.3.837
复制
发表时间:
1977-01-01
影响因子:
11.1
通讯作者:
KEZDY, FJ
KEZDY, FJ
中科院分区:
综合性期刊1区
文献类型:
--
作者:
SHEN, BW;SCANU, AM;KEZDY, FJ

文献摘要

被引文献

相似文献

对血脂正常的人血浆的脂蛋白的大小和化学组成之间的相关性的分析表明,所有循环脂蛋白的结构与半径为r的球形模型一致,其中胆固醇酯和甘油三酯的球形液核的半径为r = 20.2。被胆固醇和磷脂的单层包围,在核心的表面上具有紧密堆积的疏水末端。该内表面的平均分子面积对于磷脂为68.5埃/分子,对于胆固醇为39.1埃/分子。蛋白质在颗粒的外表面与磷脂的亲水性头部基团紧密堆积,磷脂的分子面积为62.7埃/分子,蛋白质的分子面积为15.6埃/氨基酸。游离胆固醇的极性头基不参与外层的包装,必须被蛋白质掩蔽。游离胆固醇分布在循环脂蛋白中,极高密度脂蛋白和乳糜微粒除外,根据颗粒表面曲率控制的热力学平衡。
Analysis of the correlations between size and chemical composition of lipoproteins of normolipidemic human plasma shows that the structure of all circulating lipoproteins is consistent with a spherical model of radius r in which a spherical liquid core of cholesterol esters and triglycerides of radius = r - 20.2 .ANG. is surrounded by a monolayer of cholesterol and phospholipids with closely packed hydrophobic ends on the surface of the core. The average molecular areas at this inner surface are 68.5 .ANG.2/molecule for phospholipids and 39.1 .ANG.2/molecule for cholesterol. The proteins are closely packed with the hydrophilic head groups of phospholipids at the outer surface of the particle, with molecular areas of 62.7 .ANG.2/molecule for phospholipids and 15.6 .ANG.2/amino acid for proteins. The polar head group of free cholesterol does not participate in the packing of the outer layer and must be masked by proteins. Free cholesterol is distributed among the circulating lipoproteins, with the exception of very high density lipoprotein and perhaps chylomicrons, according to a thermodynamic equilibrium governed by the curvature of the surface of the particle.