摘要

For the GalNAc alpha 1 -> specific Agaricus bisporus agglutinin (ABA) from an edible mushroom, the mechanism of polyvalent Gal beta 1 -> 3/4GlcNAc beta 1 -> complex in ABA-carbohydrate recognition has not been well defined since Gal and GlcNAc are weak ligands. By enzyme-linked lectinosorbent and inhibition assays, we show that the polyvalent Gal beta 1 -> 3/4GlcNAc beta 1 -> in natural glycans also play vital roles in binding and we propose that four different intensities of glycotopes (Gal beta 1-3GalNAc alpha 1-, GalNAc alpha 1-Ser/Thr and Gal beta 1-3/4GlcNAc beta 1-) construct three recognition systems at the same domain. This peculiar concept provides the most comprehensive mechanism for the attachment of ABA to target glycans and malignant cells at the molecular level.

  • 出版日期2010-8-20
  • 单位长春大学