ISSN:
1573-4986
Keywords:
sialyltransferase
;
galactosyltransferase
;
inhibitor
;
nucleoside monosaccharide conjugates
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The inhibition of the α-2,6-sialyltransferase from rat liver, the α-2,3-sialyltransferase from porcine submandibular gland and of the galactosyltransferase from human milk were studied using monosaccharide-, nucleoside- and nucleotide-derivatives of their naturally occurring donor substrates cytidine 5′-monophosphate-N-acetylneuraminic acid and uridine 5′-diphosphate-galactose, respectively. Only the corresponding nucleosides/nucleotides showed inhibitory activity. Periodate oxidation of CMP or CMP-Neu5Ac and of UMP or UDP-Gal led to reduced inhibitory efficiency with the respective transferase. The type and reversibility of the inhibition of some of these compounds, as well as the corresponding Ki values were determined.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1018560931389
