Reynolds J A, Tanford C
Proc Natl Acad Sci U S A. 1970 Jul;66(3):1002-7. doi: 10.1073/pnas.66.3.1002.
A wide variety of proteins have been shown to bind identical amounts of an amphiphile, sodium dodecyl sulfate, on a gram per gram basis at monomer equilibrium concentrations above 0.5 mM. The binding is independent of ionic strength and primarily hydrophobic in nature. Only the monomeric form of the amphiphile binds to proteins, not the micellar form. The application of these results to models for biological membranes and to gel electrophoresis in sodium dodecyl sulfate is discussed.
已表明,在单体平衡浓度高于0.5 mM时,多种蛋白质能以每克蛋白质结合相同量两亲物十二烷基硫酸钠。这种结合与离子强度无关,本质上主要是疏水作用。只有两亲物的单体形式能与蛋白质结合,而非胶束形式。本文讨论了这些结果在生物膜模型和十二烷基硫酸钠凝胶电泳中的应用。