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Thermal stability of oligodeoxynucleotide duplexes bound to nitrocellulose filters


Thermal stability of oligodeoxynucleotide duplexes bound to nitrocellulose filters



Analytical Biochemistry 232(2): 249-251



ISSN/ISBN: 0003-2697

PMID: 8747483

DOI: 10.1006/abio.1995.0015

The antioxidant enzyme superoxide dismutase (EC 1.15.1.1) (SOD) catalyzes the conversion of superoxide anion radical (O2.-) to hydrogen peroxide and molecular oxygen. SOD helps prevent tissue damage by O2.- and its metabolites, and augmentation of tissue SOD is a useful therapeutic strategy in certain diseases having an oxidative-injury component. Routine application of direct SOD assays is not technically facile, since the short half-life of the O2.- substrate and its free radical nature necessitate specialized analytical equipment to detect and measure O2.- chemically. Consequently, indirect SOD assays which monitor some change in an indicator substance reacting with O2.- are routinely used, particularly for biological samples. Limitations of indirect test systems utilizing heme-based indicators for the presence of O2.- and/or enzymatic O2.- generators led us to develop a SOD microassay based on spectrophotometric assessment of O2.- mediated nitro blue tetrazolium reduction by an aerobic mixture of NADH and phenazine methosulfate, which produces superoxide chemically at nonacidic pH (Rao, Free Radical Biol. Med. 7, 513-519, 1989). The proposed SOD assay system is formatted for use in an automated 96-well microplate reader and has the virtues of a nonheme indicator, a nonenzymatic O2.- source, physiological pH, and economy of time and materials. The assay has been applied to measure purified and tissue SOD (Cu,Zn- and Mn-types) activity as well as O2.- turnover by small-molecule "SOD mimetics."

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