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The Role of Ligand Density in the Enzymatic Glycosylation of Carbohydrates Presented on Self‐Assembled Monolayers of Alkanethiolates on Gold
Author(s) -
Houseman Benjamin T.,
Mrksich Milan
Publication year - 1999
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19990315)38:6<782::aid-anie782>3.0.co;2-n
Subject(s) - glycosylation , monolayer , galactosyltransferase , surface plasmon resonance , self assembled monolayer , chemistry , substrate (aquarium) , enzyme , ligand (biochemistry) , carbohydrate , biochemistry , nanotechnology , biology , materials science , nanoparticle , receptor , ecology
Abstract The biological activity of immobilized carbohydrates can show a dramatic dependence on the density of carbohydrate. This is the result of investigations with self‐assembled monolayers that present N ‐acetylglucosamine groups as a model substrate for glycosylation by bovine β ‐1,4‐galactosyltransferase (GalTase; see picture). Surface plasmon resonance spectroscopy and carbohydrate‐binding lectins were used to characterize the reaction at the interface. UDP‐Gal=uridine diphosphogalactose