Evaluation of Zn²⁺- and Cu²⁺-Binding Affinities of Native Cu,Zn-SOD1 and Its G93A Mutant by LC-ICP MS.

ABSTRACT: The tight binding of Cu and Zn ions to superoxide dismutase 1 (SOD1) maintains the protein stability, associated with amyotrophic lateral sclerosis (ALS). Yet, the quantitative studies remain to be explored for the metal-binding affinity of wild-type SOD1 and its mutants. We have investigated the demetallation of Cu,Zn-SOD1 and its ALS-related G93A mutant in the presence of different standard metal ion chelators at varying temperatures by using an LC-ICP MS-based approach and fast size-exclusion chromatography. Our results showed that from the slow first-order kinetics both metal ions Zn²⁺ and Cu²⁺ were released simultaneously from the protein at elevated temperatures. The rate of the release depends on the concentration of chelating ligands but is almost independent

SUBMITTER: Smirnova J 

PROVIDER: S-EPMC9142952 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature