High resolution two-dimensional electrophoresis and sodium dodecyl sulphate-polyacrylamide gel electrophoresis of cheese proteins after rapid solubilisation.
The proteins of cheese are rapidly solubilised by heating to 95 degrees C in buffered 2% sodium dodecyl sulfate, 5% 2-mercaptoethanol. Electrophoretic analysis of the solubilised proteins by either one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis or high resolution two-dimensional electrophoresis yields reproducible patterns characteristic of an individual cheese and its extent of ripening. The patterns reveal (i) the residual amounts of milk casein and whey proteins, and (ii) the appearance of casein degradation products, including pink-violet components as detected by Coomassie Blue staining.
Marshall
T
T
Biology Department, University of Ulster, Coleraine, Northern Ireland.
Williams
K M
KM
D002611:Cheese / Q000032:analysis*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D008722:Methods; D008894:Milk Proteins / Q000032:analysis*; D012394:Rosaniline Dyes; D012995:Solubility; D013194:Staining and Labeling
D008894:Milk Proteins; D012394:Rosaniline Dyes; C048139:Coomassie blue