Polyacrylamide gel electrophoresis of human erythrocyte membrane enzymes solubilized with triton X-100.
Human erythrocyte ghosts were solubilized in a low ionic strength medium containing 1% Triton X-100 and subjected to electrophoresis in polyacrylamide gels containing Triton X-100. Five major bands were stained with Coomassie Blue, all except one band being heterogenous when re-electrophoresed in gels containing sodium dodecyl sulphate. It was possible to detect acetylcholinesterase, non-specific esterase, ATPase, alkaline phosphatase, 5'-nucleotidase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and aldolase activities on the Triton-containing polyacrylamide gels. Two of the enzymes, ATPase and 5'-nucleotidase, showed substantial inhibition by Triton X-100 in quantitative studies. This appears to be a useful method for studying membrane enzymes in normal and pathological red cells.
D001798:Blood Proteins / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006023:Glycoproteins / Q000097:blood; D006801:Humans; D011092:Polyethylene Glycols / Q000494:pharmacology*; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology*; D012995:Solubility
D001798:Blood Proteins; D006023:Glycoproteins; D000644:Quaternary Ammonium Compounds; D011092:Polyethylene Glycols