Unknown

Dataset Information

0

L-arginine mediated renaturation enhances yield of human, ?6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.

ABSTRACT: The anti-angiogenic, carboxy terminal non-collagenous domain (NC1) derived from human Collagen type IV alpha 6 chain, [?6(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 ?6(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.

SUBMITTER: Gunda V 

PROVIDER: S-EPMC3432169 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.

Gunda Venugopal V   Boosani Chandra Shekhar CS   Verma Raj Kumar RK   Guda Chittibabu C   Sudhakar Yakkanti Akul YA  

Protein and peptide letters 20121001 10

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 differe  ...[more]

Similar Datasets

Unknown Highly effective renaturation of a streptokinase from Streptococcus pyogenes DT7 as inclusion bodies overexpressed in Escherichia coli.
| S-EPMC4026873 | biostudies-literature
Unknown Pathogenicity of missense variants affecting the collagen IV α5 carboxy non-collagenous domain in X-linked Alport syndrome.
| S-EPMC9253329 | biostudies-literature
Unknown A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV.
| S-EPMC1136898 | biostudies-other
Unknown Coiled-coil inspired functional inclusion bodies.
| S-EPMC7268670 | biostudies-literature
Unknown Partial characterization of the C-terminal non-collagenous domain (NC1) of collagen type X.
| S-EPMC1217955 | biostudies-other
Unknown Bacterial inclusion bodies contain amyloid-like structure.
| S-EPMC2494559 | biostudies-literature
Unknown Direct detection of collagenous proteins by fluorescently labeled collagen mimetic peptides.
| S-EPMC3586774 | biostudies-literature
Unknown Crucial role for the VWF A1 domain in binding to type IV collagen.
| S-EPMC4383803 | biostudies-literature
Unknown Structural diversity and domain composition of a unique collagenous fragment (intima collagen) obtained from human placenta.
| S-EPMC1154359 | biostudies-other
Unknown Inclusion bodies are a site of ebolavirus replication.
| S-EPMC3486333 | biostudies-literature