heparitin-sulfate has been researched along with 2-2--azobis(2-amidinopropane)* in 1 studies
1 other study(ies) available for heparitin-sulfate and 2-2--azobis(2-amidinopropane)
Article | Year |
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The protective effect on Cu2+- and AAPH-mediated oxidation of human low-density lipoproteins depends on glycosaminoglycan structure.
The effect of various glycosaminoglycans on Cu(2+)- and AAPH-induced oxidation of human low-density lipoprotein (LDL) was studied by monitoring conjugated diene formation. Heparin (Hep) increased the lag phase (t(lag)) of LDL oxidation, and fast moving and slow moving Hep species modified the kinetics of LDL oxidation to the same extent. Beef spleen heparan sulfate (HS) sample produced a significant increase of the t(lag) and a decrease of the conjugated diene formation of LDL whilst beef kidney HS species modified LDL oxidation kinetics to a lower extent. Dermatan sulfate (DS) from different sources caused a significant increase of the t(lag) and a decrease of the conjugated diene formation of LDL. Hyaluronic acid had no effect. Chondroitin sulfate (CS) from beef trachea produced a very strong protective antioxidant effect evaluated by increasing of the t(lag) and decreasing of the conjugated diene formation. Hep was completely ineffective in protecting LDL from 2, 2'-azobis(2-amidinopropane) hydrochloride (AAPH)-mediated oxidation, whilst DS was moderately effective. Beef trachea CS showed a very strong ability to protect LDL oxidation induced by 1 mM AAPH. The different protective effect on Cu(2+)- and AAPH-induced LDL oxidation by glycosaminoglycans is discussed considering their various structures and properties, and their capacity to interact to different extents with hydrophobic regions of LDL protein is confirmed by measuring the LDL-tryptophan fluorescence kinetics. Topics: Amidines; Animals; Cattle; Chondroitin Sulfates; Copper; Dermatan Sulfate; Glycosaminoglycans; Heparin; Heparitin Sulfate; Humans; In Vitro Techniques; Kinetics; Lipoproteins, LDL; Oxidation-Reduction; Spectrometry, Fluorescence; Structure-Activity Relationship; Swine | 1999 |