ArticleCurrent pharmaceutical biotechnology2023
Production of Recombinant Human Hybrid Ferritin with Heavy Chain and Light Chain in
Article in Current pharmaceutical biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Review
- The role of hydrogen sulfide regulation of ferroptosis in different diseases.Apoptosis : an international journal on programmed cell death · 2024Review
- Identification of Serum Ferritin-Specific Nanobodies and Development towards a Diagnostic Immunoassay.Biomolecules · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundNatural human ferritin generally contains 24 subunits with different ratios of heavy chain to light chain, and the ratio of both subunits varies depending on tissue distribution and pathological conditions. However, the production of recombinant hybrid ferritin with both subunits is more challenging.
objectiveThis study aimed to prepare the recombinant hybrid ferritin for prokaryotic expression and characterize its structure and physicochemical properties.
methodsA prokaryotic expression vector of pACYCDuet-1 harboring the two individual genes of human ferritin heavy chain and light chain (FTH/FTL-pACYCDuet-1) was constructed and transfected into Escherichia coli bacteria. Then the genes were co-induced by IPTG to express.
resultsThe ferritin was purified by hydrophobic interaction chromatography combining size exclusion chromatography and verified by mass spectrometry and characterized by spectral and morphological analysis.
conclusionFTH and FTL subunits were successfully co-assembled into a hybrid ferritin nanoparticle (rhFTH/L). The structure of rhFTH/L was demonstrated highly ordered and fairly compact. Besides, the hybrid rhFTH/L nanoparticle was shown more sensitive to thermal stress and reduced stability when compared with that of both individual rhFTH and rhFTL.
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Registered trials
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