ArticleJournal of industrial microbiology & biotechnology2012
Recovery of functionally active recombinant human phospholipid scramblase 1 from inclusion bodies using N-lauroyl sarcosine.
Article in Journal of industrial microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The Allergenic Activity of Blo t 2, aInternational journal of molecular sciences · 2023Article
- State-of-the-art and novel approaches to mild solubilization of inclusion bodies.Frontiers in bioengineering and biotechnology · 2023Review
- Are cysteine residues of human phospholipid scramblase 1 essential for PbEuropean biophysics journal : EBJ · 2021Article
- Identification and characterisation of a phospholipid scramblase in the malaria parasite Plasmodium falciparum.Molecular and biochemical parasitology · 2021Article
- Molecular cloning and biochemical characterization of the phospholipid scramblase SCRM-1 from Caenorhabditis elegans.European biophysics journal : EBJ · 2020Article
- Recovery of recombinant Mycobacterium tuberculosis antigens fused with cell wall-anchoring motif (LysM) from inclusion bodies using non-denaturing reagent (N-laurylsarcosine).BMC biotechnology · 2019Article
- Proof of concept in utilizing in-trans surface display system of Lactobacillus plantarum as mucosal tuberculosis vaccine via oral administration in mice.BMC biotechnology · 2018Article
- Identification and characterization of the novel nuclease activity of human phospholipid scramblase 1.BMC biochemistry · 2016Article
- Membrane lipid interactions in intestinal ischemia/reperfusion-induced Injury.Clinical immunology (Orlando, Fla.) · 2014Review
- N-terminal proline-rich domain is required for scrambling activity of human phospholipid scramblases.The Journal of biological chemistry · 2014Article
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Authors and funding
3 authors.
Funding
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Abstract
Human phospholipid scramblase (hPLSCR1) is a transmembrane protein involved in rapid bidirectional scrambling of phospholipids across the plasma membrane in response to elevated intracellular calcium (Ca(2+)) levels. Overexpression of recombinant hPLSCR1 in Escherichia coli BL21 (DE3) leads to its deposition in inclusion bodies (IBs). N-lauroyl sarcosine was used to solubilize IBs and to recover functionally active hPLSCR1 from them. Protein was purified to homogeneity by nickel-nitrilotriacetic acid (Ni(2+)-NTA) affinity chromatography and was >98% pure. Functional activity of the purified protein was validated by in vitro reconstitution studies, ~18% of 7-nitrobenz-2-oxa-1, 3-diazol-4-yl-phosphatidylcholine (NBD-PC) phospholipids was translocated across the lipid bilayer in the presence of Ca(2+) ions. Far ultraviolet circular dichroism (UV-CD) studies reveal that the secondary structure of protein is predominantly an α-helix, and under nondenaturing conditions, the protein exists as a monomer. Here we describe a method to purify recombinant membrane protein with higher yield than previously described methods involving renaturation techniques.
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