STUDIES OF BIOLOGIC PROPERTIES OF PROTEOGLYCANS FROM BOVINE AORTA
- 1 January 1980
- journal article
- research article
- Vol. 42 (2) , 190-196
Abstract
Chondroitin sulfate-dermatan sulfate proteoglycans (PG) were isolated from bovine aorta-intima by extraction with 4.0 M guanidinium chloride in the presence of protease inhibitors and purified through cetylpyridinium complexes. The PG were fractionated by CsCl isopycnic centrifugation into 3 fractions with different chemical composition. The anticoagulant activity of the PG fractions was studied by Stypven time, partial thromboplastin clotting time (PTT), and thrombin time assays. The 3 PG fractions delayed coagulation in the 3 assays. The PG fractions did not affect the ADP and collagen-induced platelet aggregation but inhibited the aggregation induced by 0.2 units per ml of thrombin. The PG fractions released lipoprotein lipase in rabbits when injected, and the enzyme activity released by the major PG fraction was approximately 60% of that of heparin. This PG fraction interacted with serum low density lipoproteins but not with high density lipoproteins. Certain biologic properties are probably due to the presence of dermatan sulfate in the PG fractions. Important functional roles may exist for PG in the arterial wall.This publication has 2 references indexed in Scilit:
- Characterization of bovine aorta proteoglycan extracted with guanidine hydrochloride in the presence of protease inhibitors.Journal of Biological Chemistry, 1979
- The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acidArchives of Biochemistry and Biophysics, 1961