Carbohydrate-specific antibodies in normal human sera. I. Characterization of specificity for beta-D-glucose.

A glucose-dependent hemagglutinin, present in the serum of an apparently healthy donor, is shown to be a polyclonal IgM immunoglobulin with specificity for beta-D-glucopyranose configuration. The antibody did not agglutinate erythrocytes coated with hexoses differing from glucose at C2, C3, or C4 positions or lacking the primary alcohol group at C6 position. The hemagglutination reaction, quantitated in a continuous flow system, was inhibited by the addition of 6-deoxyglucose, 5-thioglucose, 2-deoxyglucose, 2-aminoglucose or 3-0 methylglucose. D-glucose, in beta- but not in alpha-configuration, attached by a glycosidic bond to another glucose or to an aglycone, was also inhibitory. A cross-reactivity was demonstrated between glucose and 6-deoxyglucose by antibody absorption and elution techniques. The donor's serum contained independent antibodies that reacted with erythrocytes coated with melibiose, gentiobiose, cellobiose, or N-acetylmannosamine. Further investigation revealed that antibodies are present in sera of all normal adults against erythrocytes coated with melibiose and N-acetylmannosamine and with high frequency against erythrocytes coated with gentiobiose, L-rhamnose, cellobiose, D-mannose, lactose, or D-galactose.