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Glycoconjugate Journal

, Volume 13, Issue 4, pp 653–662 | Cite as

Purification and characterization of Kurloff cell sialoglycoproteins with acid phosphatase activity

  • Saïd Taouji
  • Gérard Landemore
  • Jacques Izard
Glycoconjugate Journal
  • 26 Downloads

Abstract

The majora2–6 sialoglycoproteins in detergent-extracts of Kurloff cells were purified by anion-exchange andSambucus nigra agglutinin-affinity chromatographies. The similar ultrastructural localisations of (1)S. nigra agglutinin-gold conjugates and (2) acid phosphatase activities on the Kurloff body and particularly on its myelin figures indicated that the majora2-6 sialoglycoproteins of the Kurloff cell had acid phosphatase activity. Two-dimensional electrophoresis showed that these tartrate-sensitive phosphatases corresponded to 2 acidic (pI 3.4–3.7) polypeptides of 36 and 34 kDa. Hydrolysis with peptide-N-glycosidases F gave a 33 kDa apoprotein rich in alanine, glutamic acid, tyrosine and lysin. A lectin-affinity study demonstrated that they contained hybrid type bisected and fucosylatedN-linked oligosaccharides. Cytotoxic properties were previously attributed to Kurloff cells and other studies suggested that not only acid phosphatases but alsoa2-6-linked sialic acid residues themselves may participate in natural killer activity.

Keywords

Kurloff cell acid phosphatases sialoglycoproteins lectin-blotting lectin chromatography natural killer 

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Copyright information

© Chapman & Hall 1996

Authors and Affiliations

  • Saïd Taouji
    • 1
  • Gérard Landemore
    • 1
  • Jacques Izard
    • 1
  1. 1.Laboratoire d'Histologie et de Biologie Cellulaire, UFR de MédecineUniversité de CAENFrance

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