Human Urinary Kallikrein. II. Analysis of Asparagine-Linked Oligosaccharides by Using Lectins(Biological)

  • IKEKITA MASAHIKO
    Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo
  • MASUNAGA TAKUJI
    Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo
  • KIZUKI KAZUYUKI
    Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo
  • MORIYA HIROSHI
    Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo

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Description

The patterns of micro-heterogeneity in relation to the carbohydrate structures of active- and latent-types of normal human urinary kallikrein (HUK) were analyzed by serial lectin agarose chromatographies (concanavalin A-, erythroagglutinating phytohemagglutinin-, lentil lectin- and wheat germ agglutinin-agarose chromatographies) and crossed addino-immunoelectrophoresis. In the case of active HUK, the species carrying tri- and/or tetra-aniennary oligosaccharide(s), corefucosylated bi-antennary oligosaccharidc(s), and bi-antennaiy oligosaecharides containing outer galactose residues and an N-acetylglucosamine residue linked β1,4 to a β-linked mannose residue (bisecting N-acetylglucosamine residue) amounted to approximately 36, 33 and 17% of the total active-type HUK, respectively. The micro-heterogencity of the latent-type HUK found by serial lectin affinity ehromatographies was similar to that of the active-type HUK.

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