Proteoglycans from articular cartilage of young baboons (Papio papio) were fractionated on an associative density gradient. Material from the top of the gradient was shown to contain a proteoglycan of high electrophoretic mobility on large porosity gels. Associated and/or contaminating proteins were removed by ion-exchange chromatography on DEAE-cellulose and subsequent gel filtration on Sepharose 4B in the presence of 0.1% SDS. The electrophoretically homogeneous proteoglycan (Kd 0.43 on Sepharose 4B SDS) contained 39.7% protein, was rich in aspartate, glutamate, leucine and glycine and had a GalN : GluN molar ratio of 3.87.
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