Refolding of a recombinant full-length non-structural (NS3) protein from hepatitis C virus by chromatographic procedures.
The non-structural protein 3 (NS3) of Hepatitis C virus (HCV) was expressed as inactive aggregates in Escherichia coli. The protein was refolded by chromatographic techniques of which ion exchange chromatography was best for crude samples and gel filtration best for partially purified samples. Immobilized metal ion affinity chromatography showed intermediate performance. Gradient procedures enhanced the recovery of active NS3 protein.
Li
Ming
M
National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Science, PR China.
Poliakov
Anton
A
Danielson
U Helena
UH
Su
Zhiguo
Z
Janson
Jan-Christer
JC
D002845:Chromatography / Q000379:methods*; D004789:Enzyme Activation; D004793:Enzyme Reactivators / Q000737:chemistry; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D007527:Isoenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D017361:Viral Nonstructural Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D012697:Serine Endopeptidases; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases
D004793:Enzyme Reactivators; D007527:Isoenzymes; D011994:Recombinant Proteins; D017361:Viral Nonstructural Proteins; C084422:NS3 protein, hepatitis C virus; D012697:Serine Endopeptidases; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases