Journal Article

FZJ-2018-05985

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png In Vitro Reconstitution of the Highly Active and Natively Folded Recombinant Human Superoxide Dismutase 1 Holoenzyme

Santur, K.FZJ* ; Sevenich, M.FZJ* ; Schwarten, M.FZJ* ; Nischwitz, V.FZJ* ; Willbold, D. (Corresponding author)FZJ* ; Mohrlüder, J. (Corresponding author)FZJ*

2018
Wiley-VCH Weinheim

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Please use a persistent id in citations: http://hdl.handle.net/2128/23071  doi:10.1002/slct.201801319

Abstract: SOD1 is an antioxidant enzyme that exists as a highly stable dimer in healthy humans. Each subunit contains an intramolecular disulfide bond and coordinates one zinc and one copper ion. The dimer is destabilized in the absence of the ions and disruption of the disulfide bond, which leads to the formation of small oligomers and subsequently larger insoluble aggregates. An acquired toxic function of destabilized SOD1 is postulated to be associated with amyotrophic lateral sclerosis (ALS), which is a neurodegenerative disease characterized by peripheral and central paralysis and by 3‐ to 5‐year median survival after diagnosis. In this study, we present a protocol for heterologous expression of human SOD1 in E. coli and total reconstitution of the holoenzyme, which exhibits the highest reported specific activity (four‐fold higher) of recombinant hSOD1. Biophysical characterization confirms the native state of this protein. The presented protocol provides highly active hSOD1 that will benefit in vitro investigations of this protein.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 552 - Engineering Cell Function (POF3-552) (POF3-552)

Appears in the scientific report 2018

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Database coverage:
; ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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