| 1. |
- Finne, J, et al.
(författare)
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Novel polyfucosylated N-linked glycopeptides with blood group A, H, X, and Y determinants from human small intestinal epithelial cells.
- 1989
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Ingår i: The Journal of biological chemistry. - 0021-9258. ; 264:10, s. 5720-35
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Tidskriftsartikel (refereegranskat)abstract
- A novel type of N-linked glycopeptides representing a major part of the glycans in human small intestinal epithelial cells from blood group A and O individuals were isolated by gel filtrations and affinity chromatography on concanavalin A-Sepharose and Bandeiraea simplicifolia lectin I-Sepharose. Sugar composition, methylation analysis, 1H NMR spectroscopy of the underivatized glycopeptides and FAB-mass spectrometry and electron impact-mass spectrometry of the permethylated glycopeptides indicated a tri- and tetra-antennary structure containing an intersecting N-acetylglucosamine and an alpha (1----6)-linked fucose residue in the core unit for the majority of the glycans. In contrast to most glycopeptides of other sources, the intestinal glycopeptides were devoid of sialic acid, but contained 6-7 residues of fucose. The outer branches contained the following structures: Fuc alpha 1-2Gal beta 1-3GleNAc beta 1- (H type 1) Fuc alpha 1-2Gal beta 1-4GleNAc beta 1- (H type 2) Gal beta 1-4 (Fuc alpha 1-3)GlcNAc beta 1- (X) Fuc alpha 1-2Gal beta 1-4(Fuc alpha 1-3)GleNAc beta 1- (Y) GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-3GleNAc beta 1- (A type 1) GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4GleNAc beta 1- (monofucosyl A type 2) GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4 (Fuc alpha 1-3)GlcNAc beta 1- (trifucosyl A type 2) The blood group determinant structures were mainly of type 2, whereas glycolipids from the same cells contained mainly type 1 determinants. The polyfucosylated glycans represent a novel type of blood group active glycopeptides. The unique properties of the small intestinal glycopeptides as compared with glycopeptides of other tissue sources may be correlated with the specialized functional properties of the small intestinal epithelial cells.
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| 2. |
- Hansson, Ulla-Britt, et al.
(författare)
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IgG with a deviant conformation in serum and synovial fluid from rheumatoid arthritis patients
- 1985
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Ingår i: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 22:1, s. 27-32
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Tidskriftsartikel (refereegranskat)abstract
- Specific rabbit antisera were prepared against an IgG with a special conformation (IgG spec.) previously detected in some sera from patients with rheumatoid arthritis. The antibodies had no affinity to normal human IgG and were not anti-idiotypic to human rheumatoid factor. The affinity of IgG spec, to the antibodies could not be explained by an antiglobulin activity to rabbit IgG. The amount of protein with affinity to immobilized specific IgG F(ab′)2 of the antibodies was determined in serum and synovial fluid from patients with various joint diseases. A relationship between the content of IgG spec, and the diagnosis of seropositive rheumatoid arthritis was found on analysis of serum samples. IgG spec, also occurred in synovial fluid from some individuals with seropositive rheumatoid arthritis. Differences in the serum content of IgG spec, could not be explained by differences in the normal IgG content. Circular dichroism analysis of isolated IgG spec, showed that in the region(s) close to tyrosine residue(s) this polyclonal protein had similarities to heat-aggregated IgG.
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