Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/7847
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Type: Journal article
Title: Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin
Author: Mavrangelos, C.
Thiel, M.
Adamson, P.
Millard, D.
Nobbs, S.
Zola, H.
Nicholson, I.
Citation: Protein Expression and Purification, 2001; 23(2):289-295
Publisher: Academic Press Inc
Issue Date: 2001
ISSN: 1046-5928
1096-0279
Abstract: The 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.
Keywords: Animals; Humans; Mice; Antigens, CD15; Bacterial Proteins; Escherichia coli Proteins; Immunoglobulin Fragments; DNA-Binding Proteins; Chaperonins; Molecular Chaperones; Recombinant Fusion Proteins; Flow Cytometry; Cloning, Molecular; Antigen-Antibody Reactions; Genetic Vectors; Promoter Regions, Genetic
RMID: 0020010957
DOI: 10.1006/prep.2001.1506
Appears in Collections:Paediatrics publications

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