| 1. |
- Sabharwal, H, et al.
(författare)
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Blood group specific oligosaccharides from faeces of a blood group A breast-fed infant
- 1984
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Ingår i: Molecular Immunology. - : Elsevier BV. - 1872-9142 .- 0161-5890. ; 21:11, s. 1105-1112
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Tidskriftsartikel (refereegranskat)abstract
- Four different oligosaccharides were isolated from faeces collected from a blood group A, secretor, breast-fed infant. Three of these, GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-4Glc (A-tetrasaccharide), GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-4[Fuc alpha 1-3]Glc (A-pentasaccharide) and 1-3[Fuc alpha 1-4]GlcNAc beta 1-3Gal beta 1-4Glc (A-heptasaccharide) have previously found in urine, whereas GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-3GlcNAc beta 1-3Gal beta 1-4Glc (A-hexasaccharide) is a new compound. Structures were deduced by mass spectrometry of permethylated and N-trifluoroacetylated oligosaccharide alditols. The latter gave more structural information than the corresponding N-acetyl derivatives. The four oligosaccharides were tested for blood group A activity and all were found to inhibit the binding of anti-A antibody to blood group A substance.
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| 2. |
- Kärkkäinen, T, et al.
(författare)
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Isolation and immunologic properties of a heterogeneous antigen with the characteristics of the heavy chain of human plasma kininogen
- 1982
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Ingår i: Molecular Immunology. - : Elsevier BV. - 0161-5890 .- 1872-9142. ; 19:1, s. 179-189
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Tidskriftsartikel (refereegranskat)abstract
- Kininogen antigen was purified from human plasma fraction IV by ion exchange chromatography, gel filtration and affinity chromatography with antibody specific immunoadsorbents. The immunologically pure glycoprotein had a mol. wt of approximately 60,000 and only one polypeptide chain by SDS-PAGE. An extensive charge heterogeneity by isoelectric focusing and gel filtration on polyacrylamide agarose could only in part depend on a comparatively high sialic acid content, but may be caused by differences in the carbohydrate structures sustained by lectin-binding heterogeneity on Con A-Sepharose. This antigen shares a dominating determinant with native plasma kininogens shown by complete patterns of identity in immunochemical analyses and with the monospecific antisera developed in rabbits against the heterogeneous components. The similar size, amino acid composition, low histidine content, lack of N-terminal amino acid and antigenic homogeneity fit all the so far known characteristics of the human kininogen heavy chain. Notably the antigenic determinant is resistant to degradation by activated kallikrein. This antigen with unimpaired immunologic activity may be a useful tool for preparation of antiserum for immunochemical determination of human plasma kininogen.
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| 3. |
- Syvänen, Ann-Christine, et al.
(författare)
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Conformation and sequence dependent antigenic determinants in human low molecular weight kininogen
- 1983
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Ingår i: Molecular Immunology. - : Elsevier BV. - 0161-5890 .- 1872-9142. ; 20:6, s. 669-678
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Tidskriftsartikel (refereegranskat)abstract
- Conformation and sequence-dependent antigenic determinants were investigated using a kinin-free low molecular weight kininogen isolated from Cohn's plasma fraction IV. This antigen contains the determinants of the apparently intact heavy chain common to the high molecular weight and low molecular weight kininogens. Straightforward reduction and carboxymethylation destroyed the immunoreactivity of this molecule. Antiserum prepared against the reduced protein recognized both reduced and unreduced antigen showing the presence of both types of antigenic determinant. The corresponding antibodies were separated using immunoadsorbent columns. As shown by the higher avidity of the antibodies, the conformation-dependent determinants dominate the antigenic structure.
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