Synthesis of fluorescently labelled and internally quenched UDP-Gal probes

The preparation of fluorescently labelled and internally quenched UDP-Gal probes bearing a fluorescence emitter and a quencher is described. The rate of transfer using several galactosyltransferases was examined. Our results demonstrate that galactose-modified, sugar-nucleotide-modified and double modified UDP-Gal analogues are recognized as weak substrates by blood group B α-(1→3) galactosyltransferase, α-(1→3) galactosyltransferase and milk bovine β-(1→4) galactosyltransferase.

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