Electron microscopic studies of proteoglycan aggregates from bovine articular cartilage.
Proteoglycan aggregates from bovine articular cartilage have been visualized by electron microscopy of mixed proteoglycan-cytochrome c monolayers. The proteoglycan aggregates consist of proteoglycan subunits arising laterally at fairly regular intervals (20 to 30 nm) from the opposite sides of an elongated filamentous structure. The filamentous backbone in individual aggregates varies in length from 400 to 4000 nm. The individual proteoglycan subunits in the aggregate vary in length from 100 to 400 nm. However, there is no difference in the average size of the proteoglycan subunits associated with the largest or smallest aggregates. The sizes of the individual aggregates are determined mainly by the lengths of their filamentous backbones. The stoichiometry of binding of subunits to filament, calculated from the data reported here, is close to that for the binding of subunits to hyaluronic acid reported by others.
D000818:Animals; D002358:Cartilage, Articular / Q000032:analysis*; D002417:Cattle; D003574:Cytochrome c Group; D006025:Glycosaminoglycans; D006820:Hyaluronic Acid; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D011485:Protein Binding; D011487:Protein Conformation; D011509:Proteoglycans
D003574:Cytochrome c Group; D006025:Glycosaminoglycans; D046911:Macromolecular Substances; D011509:Proteoglycans; D006820:Hyaluronic Acid