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. 1973 Jul;133(3):457–470. doi: 10.1042/bj1330457

The alkaline cleavage and borohydride reduction of cartilage proteoglycan

H Clem Robinson 1, John J Hopwood 1,*
PMCID: PMC1177724  PMID: 4270109

Abstract

A method for the rapid isolation and purification of proteoglycan by using neutral solutions of LiBr for extraction and density-gradient centrifugation is described. The effect of 0.5m-KOH on isolated proteoglycan has been studied by using NaB3H4 to reduce and label the chondroitin sulphate chains released. This study has established: (a) that at least 95% of the chondroitin sulphate chains are attached to the proteoglycan by alkali-labile bonds between xylose and serine; (b) that random degradation of the chondroitin sulphate chains does not occur to any significant extent; (c) that the method is convenient for the determination of polysaccharide number-average molecular weights.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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