LOW MOLECULAR WEIGHT SUPEROXIDE DISMUTASE IN HEART

生物体应对氧气的氧化应激 通过合成抗氧化酶来保护环境。这些酶 分子量通常在20,000到100,000之间，并且具有 作为催化成分的过渡金属或亚铁血红素。超氧化物 歧化酶清除超氧阴离子自由基保护细胞 不受激进分子的有害影响。一种新型的超氧化物 最近在心脏提取物中发现了歧化酶活性。 和肺组织。该活性被命名为ERSATZ SOD，并与 具有热稳定性、低分子量的铜矿专有配体 Mn.这项研究的总体目标是表征配体 物理和化学成分。组件(S) 将通过超滤、凝胶排斥等方法分离至均一 和离子交换层析。测定的最佳条件 用分光光度法和比色法测定催化活性 组织化学将得到发展。替身的组成 超氧化物歧化酶将通过氨基酸分析和快原子测定 轰击质谱学。紫外可见和电子 全息配体的顺磁共振波谱 将测量金属配位体络合物。配基的位置 在心脏和肺组织中可以发现 免疫细胞化学技术。 有可能将模拟的超氧化物歧化酶用作治疗 或在医学上强加的缺血期间使用分析剂- 再灌流和可能的放射防护作用 心理治疗。

Organisms cope with the oxidative stress of an oxygen environment by synthesizing antioxidant enzymes. These enzymes are usually 20,000 to 100,000 molecular weight and have either transition metals or heme as catalytic components. Superoxide dismutases scavenge the superoxide radical and protect the cell from the deleterious effects of that radical. A novel superoxide dismutase activity has recently been found in extracts of heart and lung tissue. The activity, named ersatz SOD, is associated with a heat stable, low molecular weight ligand specific for Cu or Mn. The general goal of the research is to characterize the ligand components both physically and chemically. The component(s) will be isolated to homogeneity by ultrafiltration, gel exclusion and ion exchange chromatography. Optimal conditions for assay of the catalytic activity both spectrophotometrically and histochemically will be developed. Composition of the ersatz SOD will be determined by amino acid analysis and Fast Atom Bombardment Mass Spectrometry. The uv-visible and electron paramagnetic resonance spectra of the hololigand and metalloligand complex will be measured. Location of the ligand within heart and lung tissue will be found with immunocytochemical techniques. There is the potential for use of the SOD mimic as a therapeutic or anaphalytic agent during medically imposed ischemia - reperfusion and as a possible radioprotectant during radiation therapy.