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Isolation of a Kell‐reactive protein from red cell membranes
Author(s) -
Wallas C.,
Simon R.,
Sharpe M. A.,
Byler C.
Publication year - 1986
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1986.26286152910.x
Subject(s) - membrane , dithiothreitol , elution , chemistry , chromatography , red cell , red blood cell , band 3 , membrane protein , biochemistry , enzyme , medicine
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 I 125 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.