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Novel glycolipid variations revealed by monoclonal antibody immunochemical analysis of weak ABO subgroups of A.

Artikel i vetenskaplig tidskrift
Författare Lola Svensson
Lennart Rydberg
A Hellberg
L G Gilliver
M L Olsson
S M Henry
Publicerad i Vox sanguinis
Volym 89
Nummer/häfte 1
Sidor 27-38
ISSN 0042-9007
Publiceringsår 2005
Publicerad vid Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin
Sidor 27-38
Språk en
Länkar dx.doi.org/10.1111/j.1423-0410.2005...
Ämnesord ABO Blood-Group System, chemistry, genetics, immunology, Antibodies, Monoclonal, Chromatography, Thin Layer, Genotype, Glycolipids, analysis, chemistry, Glycosyltransferases, Humans, Immunoenzyme Techniques, Lewis Blood-Group System, Phenotype
Ämneskategorier Klinisk kemi

Sammanfattning

BACKGROUND AND OBJECTIVES: The chemical basis of the subgroups of A is largely unknown. We used thin-layer chromatography immunochemical staining techniques together with a range of characterized monoclonal reagents to analyse glycolipids isolated from a variety of weak subgroups. MATERIALS AND METHODS: Glycolipids isolated from red cells collected from nine genetically defined individuals of the rare subgroups of A, including a novel A(3) allele (A(2) 539G>A) not described previously, were subjected to a highly sensitive thin-layer chromatographic immunochemical analysis. RESULTS: Semicharacterized monoclonal antibodies revealed that, in addition to the expected quantitative differences between common phenotypes and the weak subgroups, qualitative glycolipid differences (or at least an apparent qualitative basis), caused by major changes in the ratios of different structures exist. Specifically it was found that the weakest A-expressing samples (A(el) phenotype) appeared to express an unusual A structure in the 8-12 sugar region. Variable expression of several structures in one of the A weak samples were suggestive of novel blood group A structures. CONCLUSIONS: Although no structural characterization could be undertaken, the results are clearly indicative that the variant glycosyltransferases of the rare ABO subgroups are not only inefficient, but they may potentially synthesize novel ABO structures.

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