PMID: 7018082May 1, 1981Paper

Immunochemistry of the Lewis blood-group system. III. Studies on the molecular basis of the Lex property

Vox Sanguinis
H Schenkel-Brunner, P Hanfland

Abstract

The antigen specificities of different anti-Lex 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-Lea and anti-Leb sera, the antibody binding site of Lex antibodies was found to be considerably smaller, comprising merely the structure Fuc alpha leads to 4GlcNAc--R. Based on this property, homogeneously recting Lex antibodies could be isolated from heterogeneous anti-Lea + b + x sera by means of affinity chromatography of Fuc alpha leads to 4GlcNAc-Synsorb. When the serological reactivity of the purified Lex antibodies against a Lea-active glycolipid isolated from human plasma was compared with that of normal anti-Lea 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-Lex antibodies to react already with traces of Lea substance present on fetal erythrocytes, not detectable by normal anti-Lea agglutinins.

References

Jan 1, 1977·Vox Sanguinis·O P Rekvig, K Hannestad
Jan 1, 1974·Vox Sanguinis·M B Arcilla, P Sturgeon
Jul 23, 1955·Nature·J S SNEATH, P H SNEATH
Apr 1, 1956·British Journal of Haematology·M CUTBUSHP L MOLLISON
Jan 1, 1949·Acta Pathologica Et Microbiologica Scandinavica·P H ANDERSEN, K JORDAL

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Citations

Jan 1, 1984·Journal of Cellular Physiology. Supplement·F L GrahamP E Branton
Jun 1, 1982·FEBS Letters·P HanflandH Schenkel-Brunner
Jan 1, 1986·Vox Sanguinis·R OriolR Mollicone
Jan 1, 1984·Vox Sanguinis·M ContrerasB Stebbing
Jan 1, 1986·Vox Sanguinis·E B Macdonald, L M Gerns
Apr 25, 2006·FEMS Microbiology Letters·Majlis SvenssonCatharina Svanborg

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