Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/19302
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSupranee Upananen_US
dc.contributor.authorAtichat Kuadkitkanen_US
dc.contributor.authorDuncan R. Smithen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-07-12T02:29:35Z-
dc.date.available2018-07-12T02:29:35Z-
dc.date.issued2008-08-01en_US
dc.identifier.citationJournal of Virological Methods. Vol.151, No.2 (2008), 325-328en_US
dc.identifier.issn01660934en_US
dc.identifier.other2-s2.0-46949086037en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=46949086037&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/19302-
dc.description.abstractSeveral studies have identified putative dengue virus receptors using virus overlay protein binding assays (VOPBA) with some apparent success. Given that this technique relies upon the use of electrophoresis of proteins through polyacrylamide gels with varying amounts of protein denaturation, the physiological relevance of the proteins isolated is open to question. To address this issue a Sepharose 4B-dengue virus serotype 2-affinity column was constructed to selectively bind dengue virus binding proteins from HepG2 (liver) cell membrane preparations. Results show that GRP78, but not the 37/67 kDa high affinity laminin receptor, was specifically bound by the column. This result is consistent with earlier work and shows that while affinity chromatography may provide a useful adjunct to VOPBA based studies particularly in cases where proteins maybe sensitive to denaturation, proteins isolated by VOPBA can be physiologically relevant. © 2008 Elsevier B.V. All rights reserved.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=46949086037&origin=inwarden_US
dc.subjectImmunology and Microbiologyen_US
dc.titleIdentification of dengue virus binding proteins using affinity chromatographyen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.jviromet.2008.05.001en_US
Appears in Collections:Scopus 2006-2010

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.