title: Substrate heterogeneity of component a of the human erythrocyte membrane.
abstract: Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A.D., and Appel, S.H.J. Membr. Biol 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with alpha-methyl-D-glucoside does not accept the transfer of phosphate from [gamma-32 P]  ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains greater than 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J.B.C., J. Biol. Chem. 249:4398 (1974).
mesh_terms: D002462:Cell Membrane / Q000201:enzymology*; D002846:Chromatography, Affinity; D003208:Concanavalin A; D004912:Erythrocytes / Q000201:enzymology*; D006023:Glycoproteins / Q000097:blood; D006801:Humans; D010750:Phosphoproteins / Q000097:blood; D011494:Protein Kinases / Q000097:blood*
chemical_list: D006023:Glycoproteins; D010750:Phosphoproteins; D003208:Concanavalin A; D011494:Protein Kinases