ポスター発表
- 第3日 5月13日（水） P会場（1008/09）
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3P-18 PDF
ネイティブ質量分析によるSOD1の金属結合の定量解析
Cu/Zn superoxide dismutase (SOD1) is a metal enzyme that functions by binding Cu/Zn ions, and binds one zinc and one copper ion per monomer and functions as a dimer. It is also known to be involved in the pathogenesis of amyotrophic lateral sclerosis (ALS), suggesting that oxidation and dissociation of metal ions in SOD1 cause a change in conformation and involvement in the development of toxicity. Although the amount of metal in such a protein sample can be quantified by elemental analysis such as ICP, it is not easy to quantitatively determine the degree of metal binding per protein molecule such as SOD1 containing several types of metal ions of the same valence. In this study, we examined the use of native mass spectrometry to quantitatively analyze the binding state of metal ions of SOD1.