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人高密度血清脂蛋白的载脂蛋白-Gln-I和载脂蛋白-Gln-II多肽的自我缔合。

The self-association of the apo-Gln-I and apo-Gln-II polypeptides of human high density serum lipoproteins.

作者信息

Stone W L, Reynolds J A

出版信息

J Biol Chem. 1975 Oct 25;250(20):8045-8.

PMID:170279
Abstract

The major polypeptide components of human high density lipoprotein, apo-Gln-I and apo-Gln-II, self-associate at pH 8.3 and ionic strength 0.045. The dimeric (MW = 56,800) association constant for apo-Gln-I is 1.3 X 10(4)liters/mol. apo-Gln-II is tetrameric at all experimentally accessible concentrations. Self-association of apo-Gln-I is accompanied by minor conformational alterations distinct from that induced by saturating levels of bound amphiphilic ligands. These results are discussed with respect to the design of reconstitution experiments between the apoproteins and lipids.

摘要

人类高密度脂蛋白的主要多肽成分,载脂蛋白-Gln-I和载脂蛋白-Gln-II,在pH 8.3和离子强度0.045条件下会发生自缔合。载脂蛋白-Gln-I的二聚体(分子量 = 56,800)缔合常数为1.3×10⁴升/摩尔。在所有实验可及的浓度下,载脂蛋白-Gln-II都是四聚体。载脂蛋白-Gln-I的自缔合伴随着轻微的构象变化,这与由饱和水平的结合两亲性配体诱导的构象变化不同。结合载脂蛋白与脂质之间的重组实验设计对这些结果进行了讨论。

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引用本文的文献

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New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.对载脂蛋白决定高密度脂蛋白结构的新认识:专题综述系列:高密度脂蛋白结构、功能和代谢。
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Current concepts of the molecular structure and metabolism of human apolipoproteins and lipoproteins.人类载脂蛋白和脂蛋白的分子结构与代谢的当前概念。
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