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Serologic Characteristics on Phosphatidylinositol-Anchored Proteins

  • Helmut Schenkel-Brunner

Abstract

Integral membrane proteins are usually bound to the cell membrane by a transmembrane segment of amino acids which is anchored in the membrane matrix by hydrophobic interactions with the lipid components of the bilayer (see Chapter 4.1.2). A number of membrane proteins, however, are linked to the membrane by a glycosylphosphatidylinositol (= GPI) unit [22,42]. This glycolipid anchor is composed of phosphatidylinositol, a short oligosaccharide chain, and phosphatidylethanolamine (Fig. 20.1); the glycolipid anchor is connected to the C-terminal amino acid of the protein via an amide bond. This complex molecule is attached to the cell membrane by the fatty acid residues of the phosphatidylinositol moiety which are embedded in the outer leaflet of the bilayer.

Keywords

Blood Group Erythrocyte Membrane Paroxysmal Nocturnal Haemoglobinuria Blood Group Antigen Complement Regulatory Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Wien 1995

Authors and Affiliations

  • Helmut Schenkel-Brunner
    • 1
  1. 1.Institut für BiochemieUniversität WienViennaAustria

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