Polyacrylamide gel electrophoresis of several proteins in the presence of sodium oligooxyethylene dodecyl ether sulfates or a commercially available analog.
The behavior of water-soluble proteins and a typical membrane protein in polyacrylamide gel electrophoresis was studied in the presence of sodium oligooxyethylene dodecyl ether sulfates with a defined number of oxyethylene units or a commercially available analog with distribution and heterogeneity for the oxyethylene chain length and alkyl group, respectively. It was concluded that most water-soluble proteins do not interact with the anionic surfactants as long as their oxyethylene chain lengths are sufficiently long; the commercially available surfactant binds exceptionally well to beta-lactoglobulin without causing denaturation and subsequent dissociation; such surfactants are expected to solubilize membrane proteins without causing denaturation as judged from the result with Na+,K+-ATPase and are promising as new solubilizing agents for membrane proteins which enable efficient electrophoretic analysis or separation after the solubilization.
Koide
M
M
Applied Research Laboratories II, Lion Corporation, Tokyo, Japan.
Fukuda
M
M
Ohbu
K
K
Watanabe
Y
Y
Hayashi
Y
Y
Takagi
T
T
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000032:analysis; D006801:Humans; D007782:Lactoglobulins / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D011092:Polyethylene Glycols; D011506:Proteins / Q000032:analysis*; D012710:Serum Albumin, Bovine / Q000032:analysis; D012967:Sodium Dodecyl Sulfate / Q000031:analogs & derivatives*; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D012995:Solubility; D013501:Surface-Active Agents
D006454:Hemoglobins; D007782:Lactoglobulins; D008565:Membrane Proteins; D011506:Proteins; D013501:Surface-Active Agents; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; D011092:Polyethylene Glycols; D000254:Sodium-Potassium-Exchanging ATPase