Control of Solubilized State and Estimation of Molecular Organization of Membrane Proteins by the Use of Analogues of Sodium Dodecyl Sulfate

点击翻译按钮获取中文摘要

In the field of biochemical research,an anionic surfactant,sodium dodecyl sulfate(SDS),is routinely used.We have focused our attention on the potentiality of analogues of SDS of which general structure can be described as follows:n-C_<12>H_<25>(OCH_2CH_2)OSO^<3->X^+.It was found that:(1)among the analogues having their cations replaced by Li,Tris,triethanolammine and triisopropanolammine,the first was stronger even than SDS as protein denaturant,and the others were far less destructive than SDS as protein denaturant,and the others were far less destructive than SDSbecoming milder on the sequence mentioned above;(2)the series of surfactant could be used to determine the hierarchy of organization of molecular assemblies of proteins especially membrane proteins;(3)a typical example of the successful application of the series is the separation of the products of disassembly of thylakoid chlorophyllproteins in which different surfactant of the series giving different electrophoretic patterns;(4)analogues with m=2to8 were compared with to reveal that only those with m equal to or larger than 6 have high affinity to membrane proteins and thus allows efficient separation of mambrane prteins in the presence of such a surfactant;(5)a readily available surfactant similar to those described above with distribution with respect to both alkyl chain length (number of carbon atoms around 13) and oxyethylene chain length(around m =8)was found to be an efficient additive in polyacrylamide gel elctrophoresis for separation of the subunits of (Na,K)-ATPase without causing denaturation.