Determination of molecular weight of membrane proteins by the use of low-angle laser light scattering combined with high-performance gel chromatography in the presence of a non-ionic surfactant.
An assessment study was carried out to evaluate the performance of the low-angle laser light scattering technique combined with high-performance gel chromatography in the presence of a nonionic surfactant, octaethyleneglycol n-dodecyl ether, precision differential refractometry and ultraviolet photometry. It was found that the combined technique is highly promising as a method for the determination of the molecular weight of a membrane protein solubilized by the surfactant. For trial, molecular weights of the following membrane proteins of Escherichia coli, both solubilized in oligomeric forms, were measured; porin that forms the transmembrane diffusion pore in the outer membrane, and lambda-receptor protein that facilitates the diffusion of maltose-maltodextrins across the outer membrane. The result obtained indicates that both porin and lambda-receptor protein exist as trimers in the surfactant solution.
D001425:Bacterial Outer Membrane Proteins; D010582:Bacteriophage lambda / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D007834:Lasers; D008565:Membrane Proteins / Q000032:analysis*; D008823:Micelles; D008970:Molecular Weight; D018272:Porins; D011991:Receptors, Virus / Q000032:analysis; D012542:Scattering, Radiation; D013501:Surface-Active Agents
D001425:Bacterial Outer Membrane Proteins; D008565:Membrane Proteins; D008823:Micelles; D018272:Porins; D011991:Receptors, Virus; D013501:Surface-Active Agents; C016532:maltoporins