ArticleProtein and peptide letters2012
L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.
Article in Protein and peptide letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Type IV collagen derived non-collagenous domain α6 (IV) NC1 and its derivative fragments inhibit endothelial cell proliferation and attenuatesCytotechnology · 2025Article
- Cryptic collagen elements as signaling hubs in the regulation of tumor growth and metastasis.Journal of cellular physiology · 2020Review
- Developments in purification methods for obtaining and evaluation of collagen derived endogenous angioinhibitors.Protein expression and purification · 2014Review
- Inhibition of elastin peptide-mediated angiogenic signaling mechanism(s) in choroidal endothelial cells by the α6(IV)NC1 collagen fragment.Investigative ophthalmology & visual science · 2013Article
- Extra cellular matrix derived metabolite regulates angiogenesis by FasL mediated apoptosis.PloS one · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The anti-angiogenic, carboxy terminal non-collagenous domain (NC1) derived from human Collagen type IV alpha 6 chain, [α6(IV)NC1] or hexastatin, was earlier obtained using different recombinant methods of expression in bacterial systems. However, the effect of L-arginine mediated renaturation in enhancing the relative yields of this protein from bacterial inclusion bodies has not been evaluated. In the present study, direct stirring and on-column renaturation methods using L-arginine and different size exclusion chromatography matrices were applied for enhancing the solubility in purifying the recombinant α6(IV)NC1 from bacterial inclusion bodies. This methodology enabled purification of higher quantities of soluble protein from inclusion bodies, which inhibited endothelial cell proliferation, migration and tube formation. Thus, the scope for L-arginine mediated renaturation in obtaining higher yields of soluble, biologically active NC1 domain from bacterial inclusion bodies was evaluated.
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