A lectin fraction from Chardonnay grape juice has been isolated by affinity
chromatography on a column of p-aminophenyl beta-D-glucoside-derivatized a
garose. The lectin fractions agglutinate rabbit and human erythrocytes with
out serological specificity. None of the usual monosaccharides, glycosides,
or glycoproteins inhibit the hemagglutinating activity. Erythroagglutinati
on is only inhibited by nitrophenyl glycosides, p-nitrophenyl beta-D-glucos
ide being the strongest inhibitor. In SDS-PAGE in the presence of 2-mercapt
oethanol and gel filtration HPLC, the lectin fraction gave a single band or
peak corresponding to M-r 13.2-11.9 kDa, thus indicating it to be a monome
r. Three bands were observed by isoelectric focusing with pi values of 4.1,
4.4, and 4.9. The isolectins seem to be glycoproteins since they are bound
on a concanavalin A-Sepharose column.