Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin

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dc.contributor.authorMavrangelos, C.
dc.contributor.authorThiel, M.
dc.contributor.authorAdamson, P.
dc.contributor.authorMillard, D.
dc.contributor.authorNobbs, S.
dc.contributor.authorZola, H.
dc.contributor.authorNicholson, I.
dc.date.issued2001
dc.description.abstractThe success of recombinant antibody fragments as diagnostic reagents and therapeutic agents depends on the availability of sufficient functional material. We have produced a bacterial expression vector that combines high-level expression driven by a modified Shine-Dalgarno sequence with the periplasmic chaperonin Skp. Using this vector, we are able to obtain higher yields of soluble antibody fragments from cultures without the need for supplementation of the culture medium during expression. The fragments produced in the presence of the Skp show improved antigen binding activity compared to when the chaperonin is absent.
dc.identifier.citationProtein Expression and Purification, 2001; 23(2):289-295
dc.identifier.doi10.1006/prep.2001.1506
dc.identifier.issn1046-5928
dc.identifier.issn1096-0279
dc.identifier.urihttp://hdl.handle.net/2440/7847
dc.language.isoen
dc.publisherAcademic Press Inc
dc.source.urihttps://doi.org/10.1006/prep.2001.1506
dc.subjectAnimals
dc.subjectHumans
dc.subjectMice
dc.subjectBacterial Proteins
dc.subjectEscherichia coli Proteins
dc.subjectImmunoglobulin Fragments
dc.subjectDNA-Binding Proteins
dc.subjectChaperonins
dc.subjectMolecular Chaperones
dc.subjectRecombinant Fusion Proteins
dc.subjectFlow Cytometry
dc.subjectCloning, Molecular
dc.subjectAntigen-Antibody Reactions
dc.subjectGenetic Vectors
dc.subjectPromoter Regions, Genetic
dc.subjectLewis X Antigen
dc.titleIncreased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin
dc.typeJournal article
pubs.publication-statusPublished

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