Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1023686#aggregation> ?p ?o. }
Showing items 1 to 31 of
31
with 100 items per page.
- aggregation classification "A2".
- aggregation creator B436093.
- aggregation creator B436094.
- aggregation creator person.
- aggregation date "1983".
- aggregation hasFormat 1023686.bibtex.
- aggregation hasFormat 1023686.csv.
- aggregation hasFormat 1023686.dc.
- aggregation hasFormat 1023686.didl.
- aggregation hasFormat 1023686.doc.
- aggregation hasFormat 1023686.json.
- aggregation hasFormat 1023686.mets.
- aggregation hasFormat 1023686.mods.
- aggregation hasFormat 1023686.rdf.
- aggregation hasFormat 1023686.ris.
- aggregation hasFormat 1023686.txt.
- aggregation hasFormat 1023686.xls.
- aggregation hasFormat 1023686.yaml.
- aggregation isPartOf urn:issn:0250-5991.
- aggregation language "eng".
- aggregation subject "Chemistry".
- aggregation title "Some physicochemical aspects of oligosaccharide binding to concanavalin A and wheat germ agglutinin".
- aggregation abstract "The binding of fluorescently labelled carbohydrates to concanavalin A and wheat germ agglutinin was studied at equilibrium and by the stopped-flow and temperature jump relaxation methods. Ligand were mainly die 4-methylumbelliferyl glycosides of alpha (1 → 2)-linked mannooligosaccharides and of beta (1 → 4)-linked chitooligosaccharides as limited homologous series. They offer distinct advantages, parti cularly for kinetic studies. Enthalpie and kinetic considerations suggest that concanavalin A specifically binds a single mannopyranosyl group in alpha (1 →2)-linked mannooligosaccharides. This occurs preferentially at the non-reducing end. Glycosylation of a carbohydrate with e.g. an aryl group does not afect die binding kinetics and for all carbohydrates the association rate is comparable but relatively slow, which indicates that a common process is involved in the binding of all carbohydrates to concanavalin A. The affinity of a carbohydrate for concanavalin A is determined by the dissociation-rate parameter, resulting in a longer residence time for a better ligand. Interaction of chitooligosaccharides with wheat germ agglutinin is complex. With the larger members of the 4-methylumbelliferyl chitooligosaccharides, binding studies were only possible at low fractional saturation to avoid formation of unsoluble complexes. The binding kinetics of wheat germ agglutinin are faster than with concanavalin A and are consistent with a wheat germ agglutinin binding region composed of two adjacent subsites. For binding of the monoside as well as the bioside, two consistent kinetic models apply. They have common that for each ligand there exist two complexes with comparable population.".
- aggregation authorList BK760168.
- aggregation endPage "120".
- aggregation issue "suppl. 1".
- aggregation startPage "105".
- aggregation volume "5".
- aggregation isDescribedBy 1023686.
- aggregation similarTo BF02702981.
- aggregation similarTo LU-1023686.