ArticleGlycoconjugate journal2026
The structural units, recognition factors (RFs) and their codes of a LFuc Recognition Protein (FRP)
Article in Glycoconjugate journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Avidities and intensities of the Structural units, Glycotopes and their polyvalencies in the LFuc Recognition Protein (FRP)-glycan interactions have not been well defined and organized. This is due to the absence of the special glycan reagents and insufficient experiences. In this report, one of the best LFuc Recognition Proteins (FRPs) was analyzed by the enzyme-linked lectinosorbent and inhibition assays. From the data provided, it is found that the polyvalencies of the Fucα1→2Gal related structural units and their glycotopes are the dominant ones, especially these units of the human blood group H, Leb/Ley-tetra saccharide and AB-Leb/Ley-penta active glycans, but not the Lea/Lex-tri ligands and Man related units. When their intensities are expressed by Mass Relative Potency (Mass R.P.), it can be up to 5.0×105 fold higher than their key monomer (LFuc). In addition to this FRP can be a used as a powerful tool to detect the presence of the H, Leb/Ley-tetra and AB-Leb/Ley-penta glycotopes in the mammalian glycoconjugates, the theme of this report is the first constructive work of its structural units and codes for the LFuc Recognition Protein (FRP) system. It is expected to expand to reveal more others in the future.
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