BIOCHEMICAL-CHARACTERIZATION OF CANINE BLOOD-GROUP ANTIGENS - IMMUNOPRECIPITATION OF DEA-1.2, DEA-4 AND DEA-7 AND IDENTIFICATION OF A DOG ERYTHROCYTE-MEMBRANE ANTIGEN HOMOLOGOUS TO HUMAN RHESUS
A. Corato et al., BIOCHEMICAL-CHARACTERIZATION OF CANINE BLOOD-GROUP ANTIGENS - IMMUNOPRECIPITATION OF DEA-1.2, DEA-4 AND DEA-7 AND IDENTIFICATION OF A DOG ERYTHROCYTE-MEMBRANE ANTIGEN HOMOLOGOUS TO HUMAN RHESUS, Veterinary immunology and immunopathology, 59(3-4), 1997, pp. 213-223
Despite the clinical significance of the canine blood group antigens,
relatively little is known of the biochemistry of these molecules. In
this study the canine blood group antigens DEA (dog erythrocyte antige
n) 1.2, 4 and 7 were immunoprecipitated from red blood cells (RBC) bea
ring the corresponding blood group, and molecular weights of 85 kD (DE
A 1.2), 32-40 kD (DEA 4) and 53-66 kD (DEA 7) assigned. DEA 1.2 and DE
A 4 each appeared as a single band, whereas DEA 7 comprised three dist
inct bands (53, 58 and 66 kD). Polyclonal antisera specific for two pe
ptides derived from the sequence of the human Rhesus blood group (Rh30
A-C and Rh50A-C) were used in western blotting against canine and huma
n erythrocyte membranes. The Rh30A-C antiserum identified a band of mo
lecular weight 32 kD in both human and canine RBC, and the antiserum s
pecific for Rh50A-C identified a band of 38-60 kD in human membranes a
nd of 40-53 kD in canine RBC. This finding is consistent with conserva
tion of areas of the Rhesus protein sequence between human and canine
erythrocytes. (C) 1997 Elsevier Science B.V.