The collagen binding specificity of bone and platelet osteonectin is related to differences in glycosylation.

摘要: In this study we report that bone and platelet osteonectin are structurally functionally heterogeneous in terms of glycosylation collagen binding capacity. The relative sensitivity to specific glycosidases was used evaluate potential differences glycosylation. Although native electrophoretically nonidentical, N-glycanase treatment yielded products with the same apparent molecular weight. Bone also susceptible cleavage by endo H but not neuraminidase, while neuraminidase H. lectin blotting experiments osteonectin, concanavalin A bound specifically osteonectin. However, Lens culinaris agglutinin These data suggest differ their oligosaccharide side chain structures, possessing a high mannose-type complex-type structure. Solid-phase techniques were binding. types I, III, V collagen, had no affinity for these suggesting two proteins distinct.