L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.
L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.
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DOI:
10.2174/092986612802762750
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发表时间:
2012-10
影响因子:
1.6
通讯作者:
Sudhakar YA
中科院分区:
文献类型:
--
作者:
Gunda V;Boosani CS;Verma RK;Guda C;Sudhakar YA
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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影响因子:
6.4
作者:
Mundel, Thomas M.;Yliniemi, Anna-Maija;Kalluri, Raghu
通讯作者:
Kalluri, Raghu
影响因子:
8
作者:
O'Callaghan, CA;Tormo, J;Jones, EY
通讯作者:
Jones, EY
影响因子:
4.8
作者:
Petitclerc, E;Boutaud, A;Brooks, PC
通讯作者:
Brooks, PC
影响因子:
8
作者:
Reddy, RC;Lilie, H;Lange, C
通讯作者:
Lange, C
DOI:
10.1101/sqb.2002.67.255
发表时间:
2002-01-01
期刊:
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY
影响因子:
--
作者:
Kalluri, R
通讯作者:
Kalluri, R