Conformation of ferritin and apoferritin in solution. Optical rotatory dispersion properties.
Conformation of ferritin and apoferritin in solution. Optical rotatory dispersion properties.
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溶液中铁蛋白和脱铁铁蛋白的构象。
DOI：
10.1021/bi00857a017
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发表时间：
1967
期刊：
影响因子：
2.9
通讯作者：
S. Englard
中科院分区：
文献类型：
--
作者：
I. Listowsky;J. J. Betheil;S. Englard
Irving Listowsky, Joseph J. Betheil和Sasha Englard摘要：铁蛋白在600 ~ 250µ光谱范围内呈现出一种简单的光学旋转色散（ORD）曲线。在远紫外区获得的曲线在233µ处有波谷，在198µ处有波峰，这是典型的含有相当数量螺旋片段的蛋白质。利用Moffitt-Yang和Shechter-Blout对光谱可见区域的数据进行处理得到的旋转参数表明，近一半的天然蛋白质以螺旋形式存在。通过硫酸铵分馏或密度梯度离心得到不同铁含量的铁蛋白馏分。旋转性质与铁含量无关。而铁蛋白在pH 4.7下化学还原得到的载铁蛋白，
Irving Listowsky, Joseph J. Betheil, and Sasha Englard abstract: Ferritin exhibits a plain optical rotatory dispersion (ORD) curve in the spectral region from 600 to 250 µ. The curve obtained in the far-ultraviolet region with a trough at 233 µ and peakat 198 µ is typical of a protein containing an appreciable con-tent of helical segments. The rotatory parameters which were obtained using the Moffitt-Yang and Shechter-Blout treatments of the data in the visible region of the spectrum suggest that nearly halfof the native protein exists in the helical form. Ferritin fractions of varying iron content were obtained by am-monium sulfate fractionation or by density gradient centrifugation. The rotatory properties were independent of the iron content. Apoferritin prepared after chemical reduction of ferritin at pH 4.7, however,