✍ Scribed by René Csuk; Erik Prell
No coin nor oath required. For personal study only.
Selective difluorination, introducing a lactame moiety (instead of an amine) and a double bond in a trihydroxy-2-thiaquinolizidine derivative reverses the selectivity of the glycosidase inhibitor -a selective inhibitor for an a-glucosidase is altered into an excellent, competitive inhibitor for a bgalactosidase.
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Bacterial \(\beta\)-galactosidase is one of several reporter enzymes used in studying the transcriptional activity of eukaryotic promoters. Although it is one of the easiest and least expensive enzymes to assay, its use has been limited because of its low sensitivity, which is due in part to endogen
Through the use of a series of N-substituted (B-o-galactopyranosylmethyl)amines @Gal-CH,NHR) and the corresponding N-substituted C-(P-u-galactopyranosyl)formamides @Gal-CO-NHR), it has been determined that the inhibitor binding constant is influenced more by the pK, of the amine group than by the na