十二烷基和十四烷基硫酸盐在聚丙烯酰胺凝胶电泳过程中与蛋白质的相互作用。
The interaction of dodecyl and tetradecyl sulfate with proteins during polyacrylamide gel electrophoresis.
作者信息
Dohnal J C, Garvin J E
出版信息
Biochim Biophys Acta. 1979 Feb 26;576(2):393-403. doi: 10.1016/0005-2795(79)90414-8.
PMID:427196
Abstract
- The affinity of tetradecyl sulfate for many unfolded proteins is greater than that of dodecyl sulfate. 2. It is the presence of tetradecyl sulfate that results in the staining of proteins by pinacryptol yellow seen by Stoklosa and Latz (Stoklosa, J.T. and Latz, H.W. (1974) Biochem. Biophys. Res. Commun. 58, 74--79), as some tetradecyl sulfate remains associated with proteins during electrophoresis at room temperature (as opposed to dodecyl sulfate which, within the limit of detection, is completely removed). 3. Tetradecyl sulfate has a greater capacity to dissociate protein aggregates which consist of identical peptide chains, such as Glycophorin dimers and bovine serum albumin dimers, than does dodecyl sulfate.
摘要
- 十四烷基硫酸盐对许多未折叠蛋白质的亲和力大于十二烷基硫酸盐。2. 正是十四烷基硫酸盐的存在导致了斯托克洛萨和拉茨所观察到的蛋白质被片呐醇黄染色（斯托克洛萨，J.T. 和拉茨，H.W.（1974年）《生物化学与生物物理学研究通讯》58卷，74 - 79页），因为在室温下进行电泳时，一些十四烷基硫酸盐会与蛋白质保持结合（而十二烷基硫酸盐在检测限度内会被完全去除）。3. 与十二烷基硫酸盐相比，十四烷基硫酸盐解离由相同肽链组成的蛋白质聚集体（如血型糖蛋白二聚体和牛血清白蛋白二聚体）的能力更强。
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