Regulated secretion and purification of recombinant antibodies inE. coli View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-08

AUTHORS

S. Dübel, F. Breitling, I. Klewinghaus, M. Little

ABSTRACT

A plasmid for optimized protein expression of recombinant Fv antibodies (pOPE) in E. coli was used to express the variable domains of the murine monoclonal antibody HD39 specific for the human B-cell surface antigen CD22. The production of Fv antibodies by pOPE can be regulated over a wide range by varying the IPTG concentration. Antibodies that can discriminate between secreted and nonsecreted Fv antibody fragments were used to show that secretion is the limiting step for the production of functional Fv antibodies. IPTG concentrations above 20 microM increased the total antibody production, but did not yield larger amounts of secreted Fv antibodies. The addition of five histidines to the C terminus facilitates an easy single-step enrichment procedure based on immobilized metal affinity chromatography. More... »

PAGES

69-79

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02789479

DOI

http://dx.doi.org/10.1007/bf02789479

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032005049

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1285332


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