Identification of product-substrate pattern for erythrocyte membranes self-digestion using the original two-dimensional electrophoretic technique.
Ghost proteins immobilized in polyacrylamide gel after SDS-PAGE (first dimension) were degraded by endogenous membrane proteases. Fragments of the gels were submitted to SDS-PAGE (second dimension). Undigested proteins appeared on a diagonal, whereas products of proteolysis were evident below the substrates on electropherograms. The typical product patterns for spectrin, band 3, 4.1 and 4.2 proteins for human and bovine ghosts, are described.
Gaczyńska
M
M
Laboratory of Biophysics of Development and Aging, Department of Biophysics, University of łódź, Poland.
D000818:Animals; D002417:Cattle; D004586:Electrophoresis / Q000379:methods*; D010450:Endopeptidases / Q000032:analysis*; D004910:Erythrocyte Membrane / Q000032:analysis* / Q000201:enzymology; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D013997:Time Factors
D008565:Membrane Proteins; D010450:Endopeptidases