Hyperproduction of a bifunctional hybrid protein, metapyrocatechase-protein A, by gene fusion
A hybrid protein between metapyrocatechase and Staphylococcal protein A was produced by recombinant DNA techniques. A plasmid carrying the fusion gene that encodes the hybrid protein was constructed and expressed in E. coli. Over 70% of soluble proteins of the cell extracts was estimated to be the h...
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Veröffentlicht in: | Journal of biotechnology 1990-10, Vol.16 (1), p.87-96 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A hybrid protein between metapyrocatechase and Staphylococcal protein A was produced by recombinant DNA techniques. A plasmid carrying the fusion gene that encodes the hybrid protein was constructed and expressed in
E. coli. Over 70% of soluble proteins of the cell extracts was estimated to be the hybrid protein. This fusion protein is about 65000. Both the IgG-binding activity of protein A and the metapyrocatechase activity were found in the hybrid protein. The optimum pH of metapyrocatechase in the fusion protein was at around 6.5 and
K
m was 1.3 × 10
−5 M. A simple immuno-enzymometric assay was developed for anti-BSA antibody using the fusion protein. |
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ISSN: | 0168-1656 1873-4863 |
DOI: | 10.1016/0168-1656(90)90067-L |