Inhibition of hydroxyl radical-induced protein damages by trolox.
When bovine serum albumin was exposed to the hydroxyl radical generating system of ascorbate-EDTA-Fe3+ or ascorbate-EDTA-Fe(3+)-H2O2, carbonyl formation occurred. Trolox strongly inhibited the oxidative modification in a dose-dependent manner. The fragmentation and enhancement of the proteolytic susceptibility of bovine serum albumin were induced by HO. only in the presence of O2, while trolox protected the protein against such oxidative modifications. In addition, inactivations of lactate dehydrogenase and creatine kinase induced by the hydroxyl radical were also blocked by trolox.
Miura
T
T
Department of Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru, Japan.
Muraoka
S
S
Ogiso
T
T
D000332:Aerobiosis; D000693:Anaerobiosis; D000975:Antioxidants / Q000494:pharmacology*; D001205:Ascorbic Acid; D002839:Chromans / Q000494:pharmacology*; D003402:Creatine Kinase / Q000187:drug effects / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D005290:Ferric Compounds; D006861:Hydrogen Peroxide; D017665:Hydroxyl Radical / Q000037:antagonists & inhibitors*; D007770:L-Lactate Dehydrogenase / Q000187:drug effects / Q000378:metabolism; D010084:Oxidation-Reduction / Q000187:drug effects; D011506:Proteins / Q000187:drug effects*; D012710:Serum Albumin, Bovine / Q000187:drug effects
D000975:Antioxidants; D002839:Chromans; D005290:Ferric Compounds; D011506:Proteins; D012710:Serum Albumin, Bovine; D017665:Hydroxyl Radical; D004492:Edetic Acid; D006861:Hydrogen Peroxide; D007770:L-Lactate Dehydrogenase; D003402:Creatine Kinase; D001205:Ascorbic Acid; C010643:6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid