Abstract
Glycoproteins (GP) of Glanzmann's thrombasthenia (GT) and normal platelets were separated on sodium dodecyl sulphate (SDS) polyacrylamide slab gels and identified by their binding of 125I-labelled lectins having different sugar specificities. This highly sensitive technique showed that in thrombasthenic platelets, glycoproteins in the positions of IIb and III (IIIa) were greatly reduced when compared to normal platelets. After incubation with neuraminidase, IIb became undectable. GT platelet glycoproteins I, IV (IIIb), and high molecular weight GPs bound 125I-lectins more strongly than those in normal platelets, showing that there are drastic changes in the carbohydrate moieties of these major GPs.
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