Isolation and separation of proteoglycans

Details

Serval ID
serval:BIB_12982
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
Isolation and separation of proteoglycans
Journal
Journal of Chromatography. B, Biomedical Sciences and Applications
Author(s)
Savolainen H.
ISSN
1387-2273
Publication state
Published
Issued date
1999
Peer-reviewed
Oui
Volume
722
Number
1-2
Pages
255-262
Language
english
Notes
Publication types: Journal Article ; Review
Abstract
Proteoglycans contain a polypeptide core and an oligosaccharide chain composed of aminohexoses and uronic acid. The glycan chain is attached to the polypeptide in a bond to serine hydroxyl. The glycan chains may contain up to 200 disaccharide units and the proteoglycan molecular mass ranges from a few thousands to millions. Their physiological functions are related to barriers limiting diffusion across the membranes, articular lubrification, blood coagulation and cellular adhesion. The tissue proteoglycans can be extracted with 4 M guanidine hydrochloride and purified with chromatographic techniques. The soluble proteoglycans can be precipitated with cetylpyridinium chloride, purified by chromatography or by dialysis. All proteoglycan species are amenable to electrophoresis on polyacrylamide gels, and after blotting on polyvinylidene fluoride membranes, they can be stained for glycans. Proteoglycan analyses have shown their value in clinical mucopolysaccharidosis diagnostics, in occupational toxicology and in coagulation studies. Experimental applications include cell adhesion studies in tumor biology, regeneration in neurosciences or maturation of skin and kidneys.
Keywords
Animals, Humans, Proteoglycans/isolation & purification
Pubmed
Web of science
Create date
19/11/2007 12:04
Last modification date
20/08/2019 12:40
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