title: Concanavalin A binding to human erythrocytes leads to alterations in properties of the membrane skeleton.
abstract: Three properties related to the erythrocyte membrane skeleton are found to be altered after the binding of concanavalin A (Con A) to erythrocytes or their isolated membranes. Con A binding to normal erythrocytes imparts resistance to heat (49 degrees C)-induced fragmentation of the cells. The fragmentation, due to denaturation of spectrin at 49 degrees C, is prevented by Con A in a dose-dependent manner, but levels off at concentrations of Con A in excess of 100 micrograms/ml. The binding of Con A to ghosts isolated from normal, trypsin- or Pronase-treated cells prevents (completely or substantially) the elution of the skeletal protein complex when the membranes are extracted under low-ionic-strength conditions in the cold. The Con A-agglutinated membranes of trypsin- and Pronase-treated, but not normal, cells show cross-linking of skeletal proteins and band 3 with dimethyl adipimidate, a 0.86 nm (8.6 A)-span bifunctional reagent. The extent of cross-linking is greater in the Pronase-treated membrane than in the less-agglutinable trypsin-treated membranes. The results show that, after Con A has bound, rearrangements occur in the membrane that alter properties of the skeletal proteins. Additionally, redistribution of the skeletal proteins and the Con A receptor occurs in the lectin-agglutinated membranes.
authors.forename: S M
authors.initials: SM
authors.lastname: Gokhale
authors.forename: N G
authors.initials: NG
authors.lastname: Mehta
mesh_terms: D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000494:pharmacology*; D004119:Dimethyl Adipimidate / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects*; D006358:Hot Temperature; D006801:Humans; D008565:Membrane Proteins / Q000097:blood; D010447:Peptide Hydrolases / Q000494:pharmacology
chemical_list: D008565:Membrane Proteins; D003208:Concanavalin A; D004119:Dimethyl Adipimidate; D010447:Peptide Hydrolases