Conversion of egg-white lysozyme to a lectin-like protein with agglutinating activity analogous to wheat germ agglutinin.
Oligomers made of Asp-52-esterified lysozyme or native one showed agglutination for human, mouse, rat and chicken erythrocytes, and also for Hep G2 cells (liver carcinoma-derived cell line) [1] not weaker than wheat germ agglutinin (WGA). Oligomers of Asp-52-esterified lysozyme have about 4-fold stronger agglutinating activity than those of the native one. These results indicate that some enzymes can be converted to lectin-like proteins (neolectin) with binding characteristics similar to their substrate specificity.
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Department of Chemistry, Osaka University College of Science, Japan.
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D000818:Animals; D002645:Chickens; D004529:Egg White; D006384:Hemagglutination; D006801:Humans; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism* / Q000494:pharmacology; D051379:Mice; D009113:Muramidase / Q000378:metabolism*; D051381:Rats; D014407:Tumor Cells, Cultured; D014909:Wheat Germ Agglutinins / Q000494:pharmacology
D037102:Lectins; D014909:Wheat Germ Agglutinins; D009113:Muramidase