title: Cleavage of rhamnose from ristocetin A removes its ability to induce platelet aggregation.
abstract: Ristocetin A is used clinically as a tool for the measurement of von Willebrand protein due to its ability to induce the aggregation of platelets in plasma being proportional to the concentration of von Willebrand protein. The enzymatically induced cleavage of alpha-L-rhamnose from the tetrasaccharide of ristocetin A removes this ability to induce platelet aggregation in plasma, providing a possible insight into the structural basis for this effect.
authors.affiliation: University Chemical Laboratory, University of Cambridge, UK.
authors.forename: B
authors.initials: B
authors.lastname: Bardsley
authors.forename: D H
authors.initials: DH
authors.lastname: Williams
authors.forename: T P
authors.initials: TP
authors.lastname: Baglin
mesh_terms: D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010974:Platelet Aggregation / Q000187:drug effects*; D011485:Protein Binding; D012210:Rhamnose / Q000378:metabolism*; D012310:Ristocetin / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014841:von Willebrand Factor / Q000378:metabolism
chemical_list: D014841:von Willebrand Factor; D012310:Ristocetin; C016719:ristocetin A; D012210:Rhamnose