Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/15272
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dc.contributor.authorDubey, Ashok K-
dc.date.accessioned2012-12-22T20:00:21Z-
dc.date.available2012-12-22T20:00:21Z-
dc.date.issued2002-08-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/15272-
dc.description279-283en_US
dc.description.abstractPreparations of recombinant envelope glycoprotein E2 of hepatitis C virus (r-HCV E2), found to be homogeneous by N-terminal amino acid sequencing and mass spectrometry, resolved into multiple ionic species (isoforms) when analysed by isoelectric focusing (IEF) gel electrophoresis in the pI range of 3-10. These isoforms possessed pI  values in the range or 4.5-8.2. The major isoform with pI value of approximately 7. 1 was separated from the rest of them by employing a method developed on Gradiflow BF 200, a device based on preparative electrophoresis. This isoform was adjudged to be homogenous by IEF and by native polyacrylamide gel electrophoresis (PAGE).en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.39(4) [August 2002]en_US
dc.titleResolution of a complex ionic mixture of an apparently homogenous protein preparation by preparative electrophoresisen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.39(4) [August 2002]

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