Thiol-fatty acylation of the glucose transport protein of human erythrocytes.
Incubation of intact human erythrocytes with [3H]palmitate labeled a protein with electrophoretic characteristics of the glucose transporter. This labeling occurred via a thioester linkage, since it was unaffected by organic solvent extraction, but was substantially removed as the hydroxamate upon treatment with neutral hydroxylamine. Immunoprecipitation of the labeled protein with a monoclonal antibody to the glucose transporter confirmed its identity.
May
J M
JM
Department of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232-2230.
D000215:Acylation; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D008970:Molecular Weight; D009004:Monosaccharide Transport Proteins / Q000097:blood* / Q000302:isolation & purification; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000097:blood*
D006898:Hydroxylamines; D009004:Monosaccharide Transport Proteins; D010169:Palmitic Acids; D019811:Hydroxylamine; D019308:Palmitic Acid