Inhibition of solubilized superoxide dismutase co-immobilized with catalase by the polydisulfide of gallic acid.
The catalytic activity of superoxide dismutase (SOD) and its conjugates with catalase and polymer peroxidase (p-peroxidase) obtained during covalent binding of enzymes with aldehyde dextrans was indirectly characterized by inhibition of adrenaline autoxidation in 0.1 M bicarbonate buffer, pH 10.2, and in microemulsion of 0.1 M aerosol OT (AOT) and Triton X-45 in octane containing 15% aqueous phase. The polydisulfide of gallic acid (PDGA) effectively inhibited SOD and its conjugates by a mixed mechanism. The inhibition constants Ki for SOD and its conjugate (SOD-catalase)mic in 0.1 M bicarbonate buffer, pH 10.2, were 0.1 and 0.25 microM, respectively. Autoxidation of PDGA by molecular oxygen in alkaline media (pH 10.2) influenced its inhibitory properties in buffer solution and microemulsion of AOT and Triton X-45 in octane. The radical chain mechanism of co-oxidation of adrenaline and PDGA apparently includes the anion radical O2-. as a coupling agent which propagated the chain.
Eryomin
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Institute of Bioorganic Chemistry, Academy of Sciences of Belarus, Minsk, Belarus. ibochbel@eco2.iasnet.com
Losev YuP
Metelitza
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D000818:Animals; D000975:Antioxidants / Q000737:chemistry / Q000494:pharmacology; D002374:Catalase / Q000737:chemistry / Q000378:metabolism; D002417:Cattle; D004800:Enzymes, Immobilized; D004837:Epinephrine / Q000737:chemistry / Q000378:metabolism; D005707:Gallic Acid / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry; D012995:Solubility; D012996:Solutions; D013482:Superoxide Dismutase / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism
D000975:Antioxidants; D004800:Enzymes, Immobilized; D012996:Solutions; D005707:Gallic Acid; D010544:Peroxidases; D002374:Catalase; D013482:Superoxide Dismutase; D004837:Epinephrine