Human Erythrocyte Receptor of L-Fucose-specific Lectin Produced by Streptomyces sp.

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概要

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• L-Fucose-specific lectin produced by Streptomyces no. 16-3 (SFL 16-3) was labeled with N-succinimidyl-[ 2, 3-3H]-propionate to quantitatively investigate its binding to human erythrocytes. The binding inhibition by sugars was competitive, and 5 mM L-fucose or 20 mM D-mannose completely inhibited the binding. Among plant lectins, Lotus tetragonolobus, Ulex europeus I, soybean and wheat germ lectin showed competitive inhibition. The association constant and the average number of binding sites for human blood group O erythrocytes were approximately 3×107 M-1 and 1×106 cell-1, respectively. Trypsinization of erythrocytes preferentially increased the number of binding sites for human A and B erythrocytes but not for O erythrocytes. Membrane components were extracted from human B and O erythrocytes and their binding activity for SFL 16-3 was tested using the hemagglutination-inhibition assay. Poly(glycosyl)- ceramide was the predominant receptor and its fucosyl residue was essential for binding. The crude glycoprotein fraction showed only slight inhibition activity.

• 社団法人 日本農芸化学会の論文

著者

• AIDA Ko

  The Institute of Applied Microbiology, The University of Tokyo

• KAMEYAMA Toshiyuki

  The Institute of Applied Microbiology, The University of Tokyo

• OISHI Kunio

  The Institute of Applied Microbiology, The University of Tokyo

関連論文

• Human Erythrocyte Receptor of L-Fucose-specific Lectin Produced by Streptomyces sp.

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