Abstract
Protein—polysaccharide complex has been extracted with 4 M guanidinium chloride from resting and transforming-ossifying regions of calf scapula cartilage. The extract has been purified by equilibrium density gradient sedimentation and/or by polyacrylamide gel electrophoresis in different experimental conditions. The following information has been obtained so far: 1. 1.|Transforming-ossifying regions contain more protein—polysaccharide complex than the resting zone. 2. 2.|Proteoglycan subunits and a glycoprotein are the main components of the protein—polysaccharide complex. 3. 3.|The analytical composition of the protein—polysaccharide complex from the two zones is virtually identical but different types of interaction seem to exist among the components as indicated by the viscosity data and the centrifugation pattern in CsCl density gradients. 4. 4.|A highly purified preparation of the glycoprotein component from the two zones has been analyzed; the most interesting result is that only glycoprotein from the ossifying regions of cartilage reacts with murexide, showing Ca 2+ binding properties.
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