Purification and characterization of Kurloff cell sialoglycoproteins with acid phosphatase activity

• Published in: Glycoconjugate journal Vol. 13; no. 4; pp. 653 - 662
• Main Authors: Taouji, S, Landemore, G, Izard, J
• Format: Journal Article
• Language: English
• Published: United States 01-08-1996
• Subjects: Acid Phosphatase - metabolism; Chromatography, Affinity; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Glycosylation; Lectins - metabolism; Molecular Weight; Precipitin Tests; Sialoglycoproteins - isolation & purification; Sialoglycoproteins - metabolism; T-Lymphocytes, Cytotoxic - metabolism
• ISSN: 0282-0080; 1573-4986
• DOI: 10.1007/BF00731454

The major alpha 2-6 sialoglycoproteins in detergent-extracts of Kurloff cells were purified by anion-exchange and Sambucus 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 major alpha 2-6 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 fucosylated N-linked oligosaccharides. Cytotoxic properties were previously attributed to Kurloff cells and other studies suggested that not only acid phosphatases but also alpha 2-6-linked sialic acid residues themselves may participate in natural killer activity.