Binding of mitochondrial ATPase from ox heart to its naturally occurring inhibitor protein: localization by antibody binding.
The naturally occurring ATPase inhibitor protein from ox heart mitochondria was cross-linked to its binding site on the mitochondrial ATPase using 1-ethyl-3-(dimethylamino)propyl carbodiimide. The cross-linked product, when transferred electrophoretically to a nitrocellulose sheet, reacted with antibodies directed against the inhibitor protein and the beta-subunit of the ATPase. It was concluded that the binding site for the inhibitor protein lies on the beta-subunit.
D000818:Animals; D000906:Antibodies / Q000276:immunology; D001665:Binding Sites; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008929:Mitochondria, Heart / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000276:immunology / Q000378:metabolism; D000097795:ATPase Inhibitory Protein
D000906:Antibodies; D011506:Proteins; D006180:Proton-Translocating ATPases; D000097795:ATPase Inhibitory Protein