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Proteoglycans from pig aorta. Comparative study of their interactions with lipoproteins
- Source :
- Biochemical Journal; May 1986, Vol. 235 Issue: 3 p823-831, 9p
- Publication Year :
- 1986
-
Abstract
- Different proteoglycans (PGs) were isolated from pig aorta for aggregation studies with hyaluronic acid and human low-density lipoproteins (LDL). Extraction of the intima-media with 4M-guanidinium chloride and digestion of the residue with collagenase solubilized 91% of aortic hexuronic acid content. From the guanidinium chloride extract two PGs were isolated by ion-exchange and gel-permeation chromatography: proteochondroitin sulphate (PGI) with a protein-core apparent Mr of 250 000 and proteodermatan-chondroitin sulphate (PGII) with a protein-core apparent Mr of 55 000. Only PGI forms high-Mr aggregates with hyaluronic acid. From the collagenase digest two other PGs were isolated: proteoheparan sulphate and proteochondroitin sulphate (PGIII and PGIV respectively). PGIV had a smaller hydrodynamic size than PGI. PGI and PGII formed insoluble complexes with human LDL in the presence of Ca2+. PGIII or PGIV did not form precipitates with the LDL. PGI and PGII, but neither PGIII nor PGIV, were bound to LDL-Sepharose. The main peaks of PGI and PGII were eluted from LDL-Sepharose with 60 mM- and 90 mM-NaCl respectively. The results indicate that aortic PGs have different interacting potentials with lipoproteins, depending on their Mr and their glycosaminoglycan composition.
Details
- Language :
- English
- ISSN :
- 02646021 and 14708728
- Volume :
- 235
- Issue :
- 3
- Database :
- Supplemental Index
- Journal :
- Biochemical Journal
- Publication Type :
- Periodical
- Accession number :
- ejs51299068
- Full Text :
- https://doi.org/10.1042/bj2350823