Title : Inhibition of solubilized superoxide dismutase co-immobilized with catalase by the polydisulfide of gallic acid.

Pub. Date : 1997 Jul

PMID : 9331967






4 Functional Relationships(s)
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1 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. Bicarbonates superoxide dismutase 1 Homo sapiens
2 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. Bicarbonates superoxide dismutase 1 Homo sapiens
3 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. Bicarbonates superoxide dismutase 1 Homo sapiens
4 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. Bicarbonates superoxide dismutase 1 Homo sapiens