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IMMUNOCHEMICAL OBSERVATIONS ON THE HUMAN BLOOD GROUP P SYSTEM
Author(s) -
Watkins Winifred M.,
Morgan W. T. J.
Publication year - 1976
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1976.tb00552.x
Subject(s) - glycolipid , glycoprotein , trisaccharide , hydrolysis , biochemistry , chemistry , disaccharide , ceramide , monosaccharide , hemagglutination , stereochemistry , neuraminic acid , antibody , biology , immunology , apoptosis
SUMMARY Haemagglutination inhibition experiments were carried out with anti‐P 1 , anti‐P k and anti‐P sera in an attempt to increase understanding of the chemical, genetical and serological relationships within the P system. The test‐substances comprised a glycoprotein with human blood group P 1 and P k activity isolated from sheep hydatid cyst fluid, fragments isolated from the partial acid hydrolysis products of the P 1 P k active glycoprotein, glycolipids, monosaccharides and di‐ and oligosaccharides of known structure. The trisaccharide αGal(1→4)βGal(1→4)GlcNAc isolated from the glycoprotein hydrolysis products, and earlier established as the P 1 determinant (Cory et al. , 1974), was the only low molecular weight compound that gave strong inhibition with human, rabbit and goat anti‐P 1 sera. A disaccharide αGal(1→4)Gal, also isolated from the glycoprotein hydrolysis products, failed to react with anti‐P 1 reagents but inhibited human anti‐P k sera as strongly as the trisaccharide. The glycolipid αGal(1→4)βGal(1→4)Glc‐Cer (ceramide trihexoside) and other oligosaccharides containing αGal(1→4)Gal at the non‐reducing terminal were also strong inhibitors of anti‐P k sera. Oligosaccharides with terminal α‐galactosyl residues joined in other positional linkages gave definite, although less strong, inhibition. The inhibition results suggest a close structural relationship between the P 1 and P k determinants and indicate that the specificity of anti‐P k sera is less closely delineated than that of anti‐P 1 . Human anti‐P sera differed markedly from anti‐P 1 and anti‐P k and were not inhibited by any of the compounds containing α‐galactosyl residues. The glycolipid βGalNAc(1→3)αGal(1→4)βGal(1→4)Glc‐Cer (globoside) strongly inhibited the anti‐P sera. The inhibition of anti‐P k and anti‐P sera by ceramide trihexoside and globoside, respectively, confirms the observations of Naiki & Marcus (1974) and supports their conclusions that P k is the precursor of P. The genetic relationship of the P 1 antigen to P and P k is not clear but biosynthetic pathways are discussed that might explain the absence of P 1 , P k and P antigens in individuals of the p phenotype.