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Conversion of egg-white lysozyme to a lectin-like protein with agglutinating activity analogous to wheat germ
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.
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.