Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Characterisation of the a… - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Characterisation of the anti-A antibody response following an ABO incompatible (A2 to O) kidney transplantation.

Artikel i vetenskaplig tidskrift
Författare Lennart Rydberg
Michael Breimer
Jan Holgersson
Karl-Anders Karlsson
Per-Georg Nyholm
I Pascher
Lola Svensson
Bo Samuelsson
Publicerad i Molecular immunology
Volym 29
Nummer/häfte 4
Sidor 547-60
ISSN 0161-5890
Publiceringsår 1992
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin
Institutionen för de kirurgiska disciplinerna, Avdelningen för kirurgi
Sidor 547-60
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord ABO Blood-Group System, Adult, Antibody Formation, Antibody Specificity, Blood Group Incompatibility, immunology, Carbohydrate Sequence, Epitopes, chemistry, Humans, Immunoglobulin A, analysis, Immunoglobulin G, analysis, Immunoglobulin M, analysis, Kidney Transplantation, immunology, Male, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Radioimmunoassay, Time Factors
Ämneskategorier Klinisk kemi

Sammanfattning

Anti-A,B antibodies produced in a blood group OLe(a-b-) recipient receiving a kidney graft from a blood group A2Le(a-b+) donor have been analysed for their ability to bind to different glycosphingolipid antigens. Solid-phase RIA using pure glycosphingolipid antigens and a chromatogram binding assay using total nonacid glycosphingolipid fractions from erythrocytes of different human blood group phenotypes together with pure glycolipid antigens were used as assay systems. Serum antibodies were shown to bind equally well to A (types 1, 2, 3 and 4) and B (types 1 and 2) antigenic structures but no binding to H antigens (types 1, 2 and 4) was detected. After adsorption of serum antibodies on A1 Le(a-b+) erythrocytes there was a residual anti-A antibody activity which could not be adsorbed by synthetic A-trisaccharides coupled to crystalline silica (Synsorb-A). These residual antibodies, which are not present in a pretransplant serum sample, had a specificity for the A antigen with type 1 core saccharide chain and the binding epitope obviously included both the N-acetylgalactosamine and the N-acetylglucosamine. The fucose residue was apparently not obligate for binding. The conformation of the sugar units involved in the binding epitope was determined.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?