Crang A J, Rumsby M G
Biochem J. 1978 Sep 1;173(3):909-17. doi: 10.1042/bj1730909.
The mechanism for the solubilization of isolated central-nervous-system myelin by sodium dodecyl sulphate was studied in detail. The release of protein and phospholipid to the 100000 g x 1 h supernatant fraction is dependent on the total amount of detergent relative to the amount of membrane present and on the ionic strength of the solubilization system. Gel-filtration analysis of supernatant fractions indicate that at suboptimal concentrations of detergent these contain lipid-protein complexes. The complete dissociation of the individual protein components from lipid is dependent on the total amount of sodium dodecyl sulphate present in the system. The results indicate that for the analysis of membrane components in sodium dodecyl sulphate it is essential that sufficient detergent is present.
对十二烷基硫酸钠溶解离体中枢神经系统髓磷脂的机制进行了详细研究。蛋白质和磷脂释放到100000g×1h的上清液部分取决于去污剂的总量与膜量的相对关系以及溶解体系的离子强度。上清液部分的凝胶过滤分析表明,在去污剂浓度低于最佳浓度时,这些部分含有脂质 - 蛋白质复合物。单个蛋白质组分与脂质的完全解离取决于体系中十二烷基硫酸钠的总量。结果表明,对于在十二烷基硫酸钠中分析膜成分而言,存在足够的去污剂至关重要。