Abstract
IT is now generally accepted that most, if not all, of the mucopolysaccharides (MPS) in connective tissues are bound to small amounts of protein or peptide. Recent estimates indicate that this protein content may be as little as 2 per cent for hyaluronic acid and as much as 15–20 per cent for cartilage protein–polysaccharide complexes1. Crude extracts of connective tissue always contain large amounts of protein not associated with the MPS. Therefore, in almost all procedures for isolating the MPS components, deproteinization is an essential first step before purification. It is usually assumed that the variety of proteolytic enzymes used, such as pronase, papain or trypsin, specifically degrade the “unrelated” protein but do not attack that complexed to the MPS. Although this is probably true there is, nevertheless, little direct experimental evidence to support this assumption. Other methods commonly used to deproteinize crude tissue extracts are adsorption on kaolin, Lloyd's reagent, shaking with chloroform-isoamyl alcohol (Sevag's procedure) and dialysis against a cationic resin2. Besides the possibility of degradation, these procedures generally result in great losses of material.
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BERMAN, E. Separation of Connective Tissue Mucopolysaccharide–Protein Complexes from Unrelated Proteins. Nature 211, 640–641 (1966). https://doi.org/10.1038/211640a0
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DOI: https://doi.org/10.1038/211640a0