在正十二烷基八乙二醇单醚中对人血清低密度脂蛋白载脂蛋白B的表征：一项电子显微镜研究
Characterization of apolipoprotein B from human serum low density lipoprotein in n-dodecyl octaethyleneglycol monoether: an electron microscope study.
作者信息
Zampighi G, Reynolds J A, Watt R M
出版信息
J Cell Biol. 1980 Dec;87(3 Pt 1):555-61. doi: 10.1083/jcb.87.3.555.
Abstract
We have studied the structure of the totally delipidated polypeptide (apolipoprotein B [apo B]) present in low-density serum lipoprotein in detergent (n-dodecyl octaethyleneglycol monoether) solution by electron microscopy. The protein-detergent complex appears as a rod-shaped particle, 75-80 nm long and 4.5-5.5 nm wide. The volume of this particle is consistent with the previously published composition reported by Watt and Reynolds (1980, Biochemistry 19:1593-1598) of two copies of apo B and five to six equivalent micelles of detergent. The asymmetric particle possesses a high degree of flexibility and a strong tendency to self-associate in an orderly fashion. The extent of this association is pH dependent.
摘要
我们通过电子显微镜研究了去污剂（正十二烷基八乙二醇单醚）溶液中低密度血清脂蛋白中存在的完全脱脂多肽（载脂蛋白B [apo B]）的结构。蛋白质 - 去污剂复合物呈现为棒状颗粒，长75 - 80纳米，宽4.5 - 5.5纳米。该颗粒的体积与瓦特和雷诺兹（1980年，《生物化学》19:1593 - 1598）先前发表的由两个apo B拷贝和五到六个等效去污剂胶束组成的成分一致。这种不对称颗粒具有高度的柔韧性和以有序方式自缔合的强烈倾向。这种缔合程度取决于pH值。
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