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Two‐dimensional gel electrophoresis of myelin and oligodendroglial proteins solubilized by a mixture of tetramethylurea and dimethylethyleneurea
Author(s) -
Althaus HansHenner,
Klöuppner Sabine,
Poehling HansMichael,
Neuhoff Volker
Publication year - 1983
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150040507
Subject(s) - isoelectric focusing , myelin , solubilization , tetramethylurea , chemistry , chromatography , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , myelin basic protein , electrophoresis , gel electrophoresis , isoelectric point , lysis , proteolipid protein 1 , membrane protein , biochemistry , membrane , biology , enzyme , neuroscience , solvent , central nervous system
A method is introduced which allows the solubilization of membrane proteins for isoelectric focusing without prior use of sodium dodecyl sulfate. Desalted and lyophilized samples of myelin and oligodendroglial membrane proteins are readily dissolved in a mixture of tetramethylurea and dimethylethyleneurea containing lysis medium. Subsequent isoelectric focusing in polyacrylamide gels reveals that the major portion of the myelin proteins focus at a rather alkaline pH. At least 6 components of the myelin basic protein can be distinguished, demonstrating its heterogeneity. Two‐dimensional gel electrophoresis reveals that the protein composition of myelin appears to be more complex than previously stated.