前白蛋白的亚基结构。
The subunit structure of prealbumin.
作者信息
Gonzalez G, Offord R E
出版信息
Biochem J. 1971 Nov;125(1):309-17. doi: 10.1042/bj1250309.
Abstract
- Prealbumin, a thyroxine-binding protein, is known to bind also to retinol-binding protein and is suspected on X-ray-crystallographic evidence of having a quaternary structure. 2. Experiments described in this paper suggest that the molecule is a tetramer of mol.wt. about 56000, which is disaggregated with some difficulty into subunits of mol.wt. about 14000. 3. The number and staining properties of the tryptic peptides indicate that the subunits are identical or closely similar. This conclusion is reinforced by comparing the sum of the amino acid compositions of the tryptic peptides with the amino acid composition of the whole protein. All minor peptides that were isolated could be shown to be derived from major peptides. 4. No evidence has been found, either from electrophoretic experiments or from amino acid sequence determination, for any dissimilarity between the subunits.
摘要
- 前白蛋白是一种甲状腺素结合蛋白，已知它还能与视黄醇结合蛋白结合，并且根据X射线晶体学证据推测它具有四级结构。2. 本文所述实验表明，该分子是一种分子量约为56000的四聚体，将其分解为分子量约为14000的亚基存在一定困难。3. 胰蛋白酶肽段的数量和染色特性表明这些亚基是相同的或非常相似的。通过比较胰蛋白酶肽段的氨基酸组成总和与整个蛋白质的氨基酸组成，这一结论得到了加强。所有分离出的次要肽段都可证明是由主要肽段衍生而来。4. 无论是电泳实验还是氨基酸序列测定，都没有发现亚基之间存在任何差异的证据。
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本文引用的文献
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