Abstract
Purified proteoglycans from pig laryngeal cartilage were fractionated by equilibrium density gradient centrifugation in the presence of 4 M guanidinium chloride. A continuous distribution of both protein and uronic acid was observed in the gradient extending from a fraction containing most of the uronic acid to one containing one third of the protein but little uronic acid. Gel chromatography on Sepharose 2B showed all fractions to be polydisperse in size and heterogeneous in chemical composition. The chondroitin sulphate chains, however, appeared to be of the same average size in all fractions. The results imply that there are several core proteins differing in length and also in the type distribution and number of carbohydrate chains attached.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure
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