ARTICLE

Carlos Moreno ¹ and Elvin A. Kabat Ph.D.¹

¹ From the Departments of Microbiology and Neurology, College of Physicians and Surgeons, Columbia University and the Neurological Institute, Presbyterian Hospital, New York 10032.

Human antibodies to blood group A substance were purified by absorption on columns of insoluble polyleucyl hog blood group A + H substance and eluted first with N-acetylgalactosamine and then with an A active reduced pentasaccharide AR_L0.52. The M and G antibodies in these eluates were separated by density gradient centrifugation. The antibodies were studied for their relative capacities to be inhibited by various blood group A active oligosaccharides. Antibodies eluted by the N-acetylgalactosamine could be inhibited by N-acetylgalactosamine, as well as by lower concentrations of A active tri- and pentasaccharides, while those eluted by the pentasaccharide AR_L0.52 could only be inhibited by the two oligosaccharides, but not by N-acetylgalactosamine, indicating that the N-acetylgalactosamine eluate had more antibodies with smaller size combining sites than the AR_L0.52 eluate. Measurements by equilibrium dialysis gave values ranging from 2 x 10³ to 1 x 10⁵ M^–1 and the values obtained with the AR_L0.52 eluate were somewhat higher than those with the GalNAc eluate. Only one of three anti-A sera had M anti-A in the AR_L0.52 eluate, while all three had M in the N-acetylgalactosamine eluate. Data on the precipitating, hemagglutinating, complement fixing, hemolytic properties of the eluted antibodies, and of their content of and light chains are given.

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