Reassembly and reconstitution of separate αand βchains of human leukocyte antigen DR4 molecule isolated from Escherichia coli

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dc.contributor.authorJoo Hyun Kang-
dc.contributor.authorCheol-Young Maeng-
dc.contributor.authorJung Hyun Park-
dc.contributor.authorKyung Soo Hahm-
dc.contributor.authorByoung Don Han-
dc.contributor.authorKil Lyong Kim-
dc.date.accessioned2017-04-19T08:54:48Z-
dc.date.available2017-04-19T08:54:48Z-
dc.date.issued1997-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4189-
dc.description.abstractThe class II major histocompatibility complex molecules play a major role in presentation of exogenous antigenic peptides to the CD4 positive helper T cell. These are heterodimeric cell surface glycoproteins consisting of α- and β-chains. In the present study, we cloned and expressed the α- and β-chain of HLA-DR4 lacking the transmembrane and cytoplasmic domain separately in Escherichia coli using the pET-5a expression vector system. The expressed α-and β-chains were purified in a denaturing condition by an ion exchange chromatography on Q-Sepharose and a gel filtration chromatography on Sephacryl S-200, respectively. The recombinant proteins were refolded and reassembled by removing the denaturing agent and concomitant reoxidation of the disulfide bond. The refolded heterodimeric rDR4 molecule was resolved by 12.5% SDS-PAGE in a nonreducing condition and confirmed by Western blot using polyclonal antibody against DR-α and the monoclonal antibody (L243) for the conformationally correct DR molecule. The rDR4 molecules were reconstituted with a 50-fold molar excess biot-HA (307-319), and the bound peptides to the heterodimer complex were determined by a microplate assay coated with L243 antibody using Extravidin-HRP conjugate.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleReassembly and reconstitution of separate αand βchains of human leukocyte antigen DR4 molecule isolated from Escherichia coli-
dc.title.alternativeReassembly and reconstitution of separate αand βchains of human leukocyte antigen DR4 molecule isolated from Escherichia coli-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number2-
dc.citation.endPage243-
dc.citation.startPage237-
dc.citation.volume7-
dc.contributor.affiliatedAuthorJoo Hyun Kang-
dc.contributor.affiliatedAuthorCheol-Young Maeng-
dc.contributor.affiliatedAuthorJung Hyun Park-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.contributor.affiliatedAuthorKil Lyong Kim-
dc.contributor.alternativeName강주현-
dc.contributor.alternativeName맹철영-
dc.contributor.alternativeName박정현-
dc.contributor.alternativeName함경수-
dc.contributor.alternativeName한병돈-
dc.contributor.alternativeName김길룡-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 7, no. 2, pp. 237-243-
dc.subject.keywordHLA DR4 antigen-
dc.subject.keywordEscherichia coli-
dc.subject.keywordhuman-
dc.subject.keywordisolation and purification-
dc.subject.localHLA DR4 antigen-
dc.subject.localEscherichia coli.-
dc.subject.localescherichia coli-
dc.subject.localEscherichia Coli-
dc.subject.localEscherichia coli-
dc.subject.localE.coli-
dc.subject.localescherichia coil-
dc.subject.localE. coli-
dc.subject.localE. Coli-
dc.subject.localHuman-
dc.subject.localHumans-
dc.subject.localhumans-
dc.subject.localhuman-
dc.subject.localisolation and purification-
dc.description.journalClassY-
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