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Expression and characterization of a tripartite fusion protein consisting of chimeric IgG-binding receptors and beta-galactosidase
KTH, Superseded Departments, Biotechnology.
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0003-0605-8417
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0001-8993-048X
KTH, Superseded Departments, Biotechnology.
1990 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 13, no 1, 83-96 p.Article in journal (Refereed) Published
Abstract [en]

Using protein engineering, a tripartite fusion protein was constructed consisting of five IgG-binding regions of protein A from Staphylococcus aureus, two IgG-binding regions of protein G from Streptococcus strain G148 and beta-galactosidase from Escherichia coli. The resulting protein lacks the serum albumin binding regions of native protein G. The fusion protein, which is a tetramer of approximately 660 kDa, was designed as a tool for immunological assays taking advantage of its broad spectrum of antibody affinity. The gene was placed under control of two promoters, the PR promoter and the lac UV5 promoter and the expression from the two promoters was studied in a bioreactor. Induction of the PR promoter gave an intracellular product concentration corresponding to 20% of the cell dry weight. By utilizing the properties of beta-galactosidase, the protein was purified by extraction in an aqueous two-phase system. The fusion protein was not proteolytically degraded during the cultivation and purification steps. The biological activity of all three parts of the protein was demonstrated with a competitive ELISA.

Place, publisher, year, edition, pages
Elsevier, 1990. Vol. 13, no 1, 83-96 p.
National Category
Natural Sciences Engineering and Technology
URN: urn:nbn:se:kth:diva-184211DOI: 10.1016/0168-1656(90)90133-VISI: A1990CM31100006PubMedID: 1368543ScopusID: 2-s2.0-0025189739OAI: diva2:915600

NR 20160331

Available from: 2016-03-30 Created: 2016-03-30 Last updated: 2016-03-31Bibliographically approved

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