The alkaline cleavage and borohydride reduction of cartilage proteoglycan.
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 NaB(3)H(4) 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.
D000818:Animals; D001894:Borohydrides; D002356:Cartilage; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002807:Chondroitin / Q000302:isolation & purification; D006025:Glycosaminoglycans / Q000032:analysis*; D006868:Hydrolysis; D006878:Hydroxides; D008970:Molecular Weight; D009300:Nasal Septum; D010084:Oxidation-Reduction; D012694:Serine; D014461:Ultracentrifugation; D014994:Xylose
D001894:Borohydrides; D006025:Glycosaminoglycans; D006878:Hydroxides; D012694:Serine; D002807:Chondroitin; D014994:Xylose