Comparison of different myelin isolation methods by use of nonequilibrium pH gradient gel electrophoresis.
Myelin was isolated from bovine white matter by five published procedures and several modifications of two of them. Comparison of the protein profiles of the preparations by nonequilibrium pH gradient gel electrophoresis, revealed clear differences in myelin protein content and composition between preparations obtained by different methods. In isolation methods where the medium contained salts, some of the myelin proteins were solubilized, the phenomenon being most pronounced in long-period isolations in buffered CsCl solution.
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002458:Cell Fractionation / Q000379:methods*; D002499:Centrifugation, Density Gradient; D003720:Densitometry; D004586:Electrophoresis / Q000379:methods; D005782:Gels; D006863:Hydrogen-Ion Concentration; D009185:Myelin Proteins / Q000302:isolation & purification*; D009186:Myelin Sheath / Q000032:analysis
D005782:Gels; D009185:Myelin Proteins