The Mass Spectrometry society of Japan - The 68th Annual Conference on Mass Spectrometry, Japan
Japanese

Abstract

Table of contents

Timetable

Plenary Lectures

Oral Sessions (Day1, Day2, Day3)

Poster Presentations (Day1, Day2, Day3)

Workshops

Luncheon Seminars (Day1, Day2, Day3)

Poster Presentations

Day 3, May 13（Wed.）　　Poster (1008/09)

3P-18　　PDF

Quantitative analysis of SOD1 metal binding by native mass spectrometry

(1Yokohama City Univ., 2Keio Univ)
oMichiko Tajiri1, Nanako Azegami1, Yoshiaki Furukawa2, Satoko Akashi1

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.