Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 84, Issue -, Pages 108-114Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2012.02.002
Keywords
Poly-LacNAc; Glycosyltransferases; beta 1,4-galactosyltransferase; beta 1,3-N-acetyl-glucosaminyltransferase; Galectin
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Poly-N-acetyllactosamines (poly-LacNAc, [-3Gal(beta 1-4)GlcNAc(beta 1-](n)) are terminal glycan structures present in glycoproteins and glycolipids. Their biological functions as ligands for galectins and as carriers of glycan epitopes are well documented. In the present paper we have characterized six novel functionalized beta-D-GlcNAc derivatives, including aglyca of varying hydrophobicity and molecular weight, as substrates for recombinant human beta 1,4 galactosyltransferase 1 (beta 4GalT-1). The sugar derivatives carry short or long amino- or azide-terminated linker molecules for further modification or immobilization. The linker chemistry had an impact on enzyme kinetics and enzymatic syntheses of N-acetyllactosamine derivatives (LacNAc, Gal(beta 1-4)GlcNAc(beta 1-R). The combination of beta 4GaIT-1 with bacterial beta 1,3-N-acetylglucosaminyltransferase (beta 3GlcNAc-T) resulted in the preparative syntheses of LacNAc oligomers with up to three LacNAc repeating units. All products were characterized by NMR and MS. The obtained LacNAc glycans were immobilized onto microtiter plates and their efficiency of binding of fungal galectin CGL2 was determined. (C) 2012 Elsevier B.V. All rights reserved.
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