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Immunochemistry of the Lewis Blood‐Group System
Author(s) -
SchenkelBrunner H.,
Hanfland P.
Publication year - 1981
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1981.tb00721.x
Subject(s) - immunoadsorption , immunochemistry , antibody , hemagglutination , chemistry , abo blood group system , antigen , serology , glycolipid , polyclonal antibodies , epitope , microbiology and biotechnology , biochemistry , biology , immunology
. The antigen specificities of different anti‐Le x sera were examined by immunoadsorption 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 Fuc α1→ 4GlcNAc‐R . Based on this property, homogeneously reacting Le x antibodies could be isolated from heterogeneous anti‐Le a+b+x+ sera by means of affinity chromatography on Fuc α1→ 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 Le x character of cord blood erythrocytes is not based on the existence of a separate Le x 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.