Isolation and separation of proteoglycans

Proteoglycans contain a polypeptide core and an oligosaccharide chain compo sed of aminohexoses and uronic acid. The glycan chain is attached to the po lypeptide in a bond to serine hydroxyl. The glycan chains may contain up to 200 disaccharide units and the proteoglycan molecular mass ranges from a f ew thousands to millions. Their physiological functions are related to barr iers limiting diffusion across the membranes, articular lubrification, bloo d coagulation and cellular adhesion. The tissue proteoglycans can be extrac ted with 4 M guanidine hydrochloride and purified with chromatographic tech niques. The soluble proteoglycans can be precipitated with cetylpyridinium chloride, purified by chromatography or by dialysis. All proteoglycan speci es are amenable to electrophoresis on polyacrylamide gels, and after blotti ng on polyvinylidene fluoride membranes, they can be stained for glycans. P roteoglycan analyses have shown their value in clinical mucopolysaccharidos is diagnostics, in occupational toxicology and in coagulation studies. Expe rimental applications include cell adhesion studies in tumor biology, regen eration in neurosciences or maturation of skin and kidneys. (C) 1999 Elsevi er Science B.V. All rights reserved.