The antigen specificities of different anti-Lex sera were examined by immu- noadsorption studies using adsorbents with well-defined carbohydrate units covalently bound to an inorganic matrix (Synsorb®, Chembiomed). In contrast to those of normal anti-Le^a and anti-Le^b sera, the antibody binding site of Le^x antibodies was found to be considerably smaller, comprising merely the structure Fucal→4GlcNAc-R. Based on this property, homogeneously reacting Lex antibodies could be isolated from heterogeneous anti-Le^a+b+x+ sera by means of affinity chromatography on Fucal→4GlcNAc-Synsorb. When the serological reactivity of the purified Le^x antibodies against a Le^a-active glycolipid isolated from human plasma was compared with that of normal anti-Le^a serum using haemagglutination inhibition and quantitative passive haemagglutination tests, evidence was obtained that the Lex character of cord blood erythrocytes is not based on the existence of a separate Lex antigen, but rather on the ability of the anti-Le^x antibodies to react already with traces of Le^a substance present on fetal erythrocytes, not detectable by normal anti-Le^a agglutinins.

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1981
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