ArticleWorld journal of microbiology & biotechnology2020
Molecular characterization, purification, and antioxidant activity of recombinant superoxide dismutase from the Pacific abalone Haliotis discus hannai Ino.
Article in World journal of microbiology & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Embryotoxicity and Spermiotoxicity of Green- and Chemically Synthesized Titanium Dioxide Nanoparticles in the Sea Urchin Paracentrotus lividus.Biological trace element research · 2026Article
- Multifaceted roles of superoxide dismutases (SODs) in cellular homeostasis and cancer progression: Redox regulation and therapeutic implications.Journal of medical biochemistry · 2026Article
- Non-lethal heat shock unlocksFrontiers in immunology · 2026Article
- Cloning, characterization, and spatio-temporal expression patterns of HdhSPARC and its responses to multiple stressors.Scientific reports · 2024Article
- Molecular Cloning and Functional Characterization of Catalase in Stress Physiology, Innate Immunity, Testicular Development, Metamorphosis, and Cryopreserved Sperm of Pacific Abalone.Antioxidants (Basel, Switzerland) · 2023Article
- Molecular Characterization of a New Tetrodotoxin-Binding Protein, Peroxiredoxin-1, fromInternational journal of molecular sciences · 2022Article
- Recent Progress in Antioxidant Active Substances from Marine Biota.Antioxidants (Basel, Switzerland) · 2022Review
- Multi-Omics Analysis of Gene and Protein Candidates Possibly Related to Tetrodotoxin Accumulation in the Skin ofMarine drugs · 2021Article
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Authors and funding
10 authors.
Funding
Abstract
Superoxide dismutase (SOD) is an acidic metalloenzyme that scavenges free radicals produced by endogenous and exogenous substances. In the present study, the tissue distribution of the superoxide dismutase HdhCu/Zn-SOD was investigated in Haliotis discus hannai Ino. The expression profile after lipopolysaccharide (LPS) challenge was determined using quantitative real-time polymerase chain reaction (qPCR). To study the antioxidant activity of a recombinant HdhCu/Zn-SOD protein, the HdhCu/Zn-SOD gene was cloned into the pPIC9K vector and transformed into the Pichia pastoris GS115 strain by electroporation. After induction by methanol, the recombinant product was purified using immobilized metal affinity chromatography and confirmed using mass spectrometry. The optimal expression conditions were determined to be incubation with 0.5% methanol at pH 6.0, resulting in a stable expressed product with the molecular weight of approximately 17 kDa and 21 kDa. The enzymatic activity of HdhCu/Zn-SOD consistently increased with increasing Cu
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