Interactions of lectins with (Na+ + K+)-ATPase of eel electric organ.
Interaction of lectins with a detergent-solubilized ATPase from eel electric organ was studied. Concanavalin A, which binds to alpha-mannosides, altered the rate of enzyme migration in agar and inhibited the formation of an antigen-antibody precipitate: other lectins had no such effects. Concanavalin A similar amounts partially inhibited (Na+ + K+)-ATPase; this inhibition was reversible by alpha-methylglucoside. There was no corresponding effect of concanavalin A on the potassium p-nitrophenylphosphatase. Concanavalin A also did not interfere with ouabain binding. Thus, concanavalin A binds to an antigenic region also involved in Na+ and/or ATP binding, but does not interact with a K+ site.
D009597:4-Nitrophenylphosphatase / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001666:Binding Sites, Antibody; D003208:Concanavalin A; D004524:Eels; D004557:Electric Organ / Q000187:drug effects / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D005779:Immunodiffusion; D007700:Kinetics; D008861:Microsomes / Q000187:drug effects / Q000201:enzymology; D010042:Ouabain / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D011485:Protein Binding; D012964:Sodium / Q000494:pharmacology
D003208:Concanavalin A; D010042:Ouabain; D012964:Sodium; D009597:4-Nitrophenylphosphatase; D000251:Adenosine Triphosphatases; D011188:Potassium