首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >The structure of human apolipoprotein E2, E3 and E4 in solution. 2. Multidomain organization correlates with the stability of apoE structure.
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The structure of human apolipoprotein E2, E3 and E4 in solution. 2. Multidomain organization correlates with the stability of apoE structure.

机译:溶液中人载脂蛋白E2,E3和E4的结构。 2.多域组织与apoE结构的稳定性有关。

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摘要

The stabilities toward thermal and chemical denaturation of three recombinant isoforms of human apolipoprotein E (r-apoE2, r-apoE3 and r-apoE4), human plasma apoE3, the recombinant amino-terminal (NT) and the carboxyl-terminal (CT) domains of plasma apoE3 at pH 7 were studied using near and far ultraviolet circular dichroism (UV CD), fluorescence and size-exclusion chromatography. By far UV CD, thermal unfolding was irreversible for the intact apoE isoforms and consisted of a single transition. The r-apoE3 was found to be less stable as compared to the plasma protein and the stability of recombinant isoforms was r-apoE4
机译:人类载脂蛋白E的三种重组同工型(r-apoE2,r-apoE3和r-apoE4),人血浆apoE3,重组氨基末端(NT)和羧基末端(CT)结构域对热和化学变性的稳定性使用近紫外和远紫外圆二色性(UV CD),荧光和尺寸排阻色谱法研究了pH 7下血浆apoE3的含量。到目前为止,UV CD对完整的apoE亚型而言是不可逆的热展开,它由一个过渡组成。与血浆蛋白相比,发现r-apoE3不稳定,重组同工型的稳定性为r-apoE4

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