An easy method for bacterial expression and purification of wild-type and mutant superoxide dismutase 1 (SOD1)

Protein Expr Purif. 2017 Jun:134:63-71. doi: 10.1016/j.pep.2017.04.001. Epub 2017 Apr 3.

Authors

Babila J Tachu¹, Katharina A Wüsten¹, Maria C Garza², Holger Wille², Gültekin Tamgüney³

Affiliations

¹ German Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Straße 27, 53127 Bonn, Germany.
² Centre for Prions and Protein Folding Diseases & Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada.
³ German Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Straße 27, 53127 Bonn, Germany. Electronic address: [email protected].

PMID: 28385582
DOI: 10.1016/j.pep.2017.04.001

No abstract available

Keywords: Aggregation; Amyloid; Amyotrophic lateral sclerosis (ALS); Enzyme activity; Oligomers; SOD1.

MeSH terms

Cell Line
Cloning, Molecular / methods*
Electrophoresis, Polyacrylamide Gel / methods
Escherichia coli / genetics*
Humans
Models, Molecular
Mutation
Protein Aggregates
Superoxide Dismutase-1 / chemistry
Superoxide Dismutase-1 / genetics*
Superoxide Dismutase-1 / isolation & purification
Superoxide Dismutase-1 / metabolism

Substances

Protein Aggregates
Superoxide Dismutase-1