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Serological and immunochemical characterization of anti-PP1Pk (anti-Tja) antibodies in blood group little p individuals. Blood group A type 4 recognition due to internal binding.

Rydberg, Lennart, 1944 (författare)
Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin,Institute of Laboratory Medicine, Dept of Clinical Chemistry/Transfusion Medicine
Cedergren, B (författare)
Breimer, Michael, 1951 (författare)
Gothenburg University,Göteborgs universitet,Institutionen för de kirurgiska disciplinerna, Avdelningen för kirurgi,Institute of Surgical Sciences, Department of Surgery
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Lindström, K (författare)
Nyholm, Per-Georg, 1958 (författare)
Samuelsson, B E (författare)
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 (creator_code:org_t)
1992
1992
Engelska.
Ingår i: Molecular immunology. - 0161-5890. ; 29:10, s. 1273-86
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Serum samples from 13 blood group little p individuals were tested by radioimmunoassay for their IgG antibody subclass distribution against the P, P1 and Pk antigens. There was no uniform subclass distribution pattern, although all but one had IgG3 antibodies against all the P system antigens tested. Studies were performed adsorbing anti-Tja serum sequentially to columns with synthetic carbohydrate antigenic determinants within the P system coupled to silica beads (SynsorbsR). The effect on agglutinin and indirect antiglobulin titers was determined after adsorption to SynsorbsR with different P-system antigens (P1, Pk, P). Adsorption to all the three SynsorbsR was needed to eliminate or strongly reduce antibody titers. The effect on IgM, IgG, IgA as well as IgG subclass antibody binding to P, P1 and Pk antigens was also determined by radioimmunoassay and chromatogram binding assay. Anti-PP1Pk antibodies from a little p woman with repeated abortions were shown to bind to glycosphingolipid antigens prepared from one of the aborted placentae using a chromatogram binding assay. This binding was eliminated by serum adsorption to SynsorbsR with P1, Pk and P carbohydrates. Anti-PP1Pk antibodies were also shown to bind to extended structures in the globoseries, i.e. globopentaosylceramide, globohexaosylceramide (globo-H) and globoheptaosylceramide (globo-A). This binding is most probably due to antibodies recognizing internal sequences in the carbohydrate chain. Attempts were made to visualize the binding epitope of the antibodies by computer molecular modelling.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine (hsv//eng)

Nyckelord

Adult
Aged
Agglutinins
immunology
Antibodies
Anti-Idiotypic
immunology
Carbohydrate Sequence
Chromatography
High Pressure Liquid
Female
Glycolipids
immunology
Humans
Immunoglobulin A
immunology
Immunoglobulin G
analysis
immunology
Immunoglobulin M
immunology
Isoantibodies
analysis
Male
Middle Aged
Models
Molecular
Molecular Conformation
Molecular Sequence Data
P Blood-Group System
immunology
Radioimmunoassay

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