Abnormal blood group galactosyltransferase in blood type A1B-subjects whose sera contain anti-B agglutinin.

A blood type A1B female, whose plasma agglutinates B red blood cells from other subjects but not her own, was found. Her sister with blood type A1B (sister-1) exhibited the same peculiarity. The agglutination titer of red cells from these two subjects is lower than that of normal B. Her father is blood type B, and his plasma did not agglutinate B red cells from other subjects and his own. Her mother and another sister (sister-2) were usual blood type A1. Blood group galactosyltransferase (B-enzyme) activity of plasma from the propositus, sister-1, and their father was very low. Km for 2'-fucosyllactose of B-enzyme of these subjects was 1.3 mM, which was more than two times higher than that of the normal value. Km for UDP-Gal was similar, but the pH-activity profile differed for the two enzymes. Red cell membranes from her father contained about 70% ungalactosylated H-sites, whereas, virtually all H-sites are galactosylated in the usual B red cell membranes. The blood group ABH components are known to be heterogeneous. Because of the abnormal B-enzyme with low activity and low substrate affinity, some H components might not be galactosylated, particularly in A1B cases (i.e., the propositus and her sister-1), due to competition by A1 enzyme. The lack of certain B components is likely to be the cause of the existence of the anti-B agglutinin in their sera.