Isolation of a Kell-reactive protein from red cell membranes.
A red cell membrane protein which exhibits Kell blood group antigen activity has been identified with a purified anti-Kell bound to a Protein-A agarose column and eluting with lithium diiodosalicylate (LIS). Although anti-Kell as well as the Kell-reactive membrane protein were eluted from the column, the eluate was capable of reducing the titer of added anti-Kell from 64 to 4. In addition, the eluate was shown to possess Kell reactivity by binding I125 Protein A after incubation with anti-Kell. Electrophoresis (SDS gel polyacrylamide 5-20% gradient) showed a band at approximately 90,000 daltons when solubilized membranes from Kell-positive red cells were used but not when membranes from dithiothreitol- and papain-treated Kell-positive red cells or Kell-negative red cells were used. A band isolated with unreduced conditions was capable of neutralizing anti-Kell.
D001457:Anion Exchange Protein 1, Erythrocyte / Q000276:immunology; D001789:Blood Group Antigens; D004910:Erythrocyte Membrane / Q000276:immunology*; D006801:Humans; D007519:Isoantigens / Q000302:isolation & purification*; D007626:Kell Blood-Group System; D008565:Membrane Proteins / Q000276:immunology; D008970:Molecular Weight; D009500:Neutralization Tests
D001457:Anion Exchange Protein 1, Erythrocyte; D001789:Blood Group Antigens; D007519:Isoantigens; D007626:Kell Blood-Group System; D008565:Membrane Proteins