鸡心脱辅基细胞色素c的疏水相互作用和折叠倾向
Hydrophobic interaction and folding propensity of chicken heart apocytochrome c.
作者信息
Tong J C, Yi P, Yang F Y
机构信息
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
出版信息
Biochem Mol Biol Int. 1995 Aug;36(6):1177-86.
In contrast to horse heart apocytochrome c, the chicken one showed quite different folding propensity as titrated by NaCl at different pH. At pH 2.0, folding behaviour of both apocytochrome c are essentially similar; while at pH higher than 4.0, chicken heart apocytochrome c has much enhanced propensity to fold and aggregate, as was shown by circular dichroism spectra, intrinsic fluorescence and non-denatured polyacrylamide gel electrophoresis. Hydrophobic chromatography demonstrated much higher hydrophobicity of chicken heart apocytochrome c, thus strongly suggested that it is the hydrophobic interaction that stabilize the 'Molten Globule' like, partially-folded structure of chicken heart apocytochrome c at neutral pH.
与马心脱辅基细胞色素c相比，在不同pH值下用NaCl滴定的鸡心脱辅基细胞色素c表现出截然不同的折叠倾向。在pH 2.0时，两种脱辅基细胞色素c的折叠行为基本相似；而在pH高于4.0时，鸡心脱辅基细胞色素c具有更强的折叠和聚集倾向，圆二色光谱、内源荧光和非变性聚丙烯酰胺凝胶电泳结果均表明了这一点。疏水色谱法显示鸡心脱辅基细胞色素c具有更高的疏水性，因此强烈表明，在中性pH值下，正是疏水相互作用稳定了鸡心脱辅基细胞色素c类似“熔球态”的部分折叠结构。
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