Heparin trisaccharides with nonreducing 2-amino-2-deoxy-alpha-D-glucopyranosyl end-groups suitable as substrates for catabolic enzymes.
Heparin trisaccharides having the sequence O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-(1----4)-O-alpha-L- idopyranosyluronic acid-(1----4)-2,5-anhydro-D-[1-3H]mannitol have been prepared, as substrate models for studying sulfatases of heparan sulfate catabolism, by alpha-L-iduronidase cleavage of previously reported heparin tetrasaccharides, with additional chemical and enzymic modification as required. Three series are described, including isomeric sulfate esters of that trisaccharide with no N-substituent, with N-acetyl substitution, and with N-sulfate substitution. New features of the substrate specificity of the hydrolases used, including iduronate sulfatase, alpha-L-iduronidase, glucosamine 6-sulfate sulfatase, and heparin sulfamidase, were observed, and simple procedures for partial purification of these hydrolases are reported. The structures assigned to the trisaccharides are supported by the mode of preparation, reactions, regularities in electrophoretic behavior, and identities of the products of deamination.
D002240:Carbohydrate Sequence; D005944:Glucosamine / Q000031:analogs & derivatives* / Q000138:chemical synthesis; D006493:Heparin; D006867:Hydrolases / Q000378:metabolism*; D007536:Isomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014312:Trisaccharides / Q000138:chemical synthesis*
D014312:Trisaccharides; D006493:Heparin; D006867:Hydrolases; D005944:Glucosamine