[The substantination of isotypical differentiation in AB0 system against nonagglutinogenic acid glycotopes of lipid origin]

Monoclonal reagents from Workshop IV were inhibited by glucoconjugates obtained from the membranes of 3 samples of AB (erythrocytes of different isotypes) by enzymatic treatment and the chloroform-methanol method and tested both serologically and in cell electrophoresis by a change of electrophoretic motility under the influence of antibodies and the complement. Glycoconjugates of the lipid and protein origin were additionally subjected to separation by the ion-exchange column chromatography on fractions of the alkaline and acid types. The differences developed in the inhibiting ability of the acid fractions of A and B antigens. The activity of glycoprotein fraction Apr-3 correlating with the difference in the agglutianability of A1 and A2. For glycolipid A1p-3, on the contrary, it turned out to be more expressed in A2B than in A1B, and it correspondent to electrophoretically revealed differences (A(c'+) in A2B and A(c'-) in A1B). In an A2B donor (A(c'-) B(c'-)) this dependens developed too. The antigenic differences of A and B glycotopes depending upon their origin (protein or lipid) and isoelectric properties are not cofined to erythrocyte agglutinogenity and should be taken into account it the system of isotypical differentiation of AB0.