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      Interaction of the Two Proteins of the Methoxylation System Involved in Cephamycin C Biosynthesis : IMMUNOAFFINITY, PROTEIN CROSS-LINKING, AND FLUORESCENCE SPECTROSCOPY STUDIES

        , , ,
      Journal of Biological Chemistry
      American Society for Biochemistry & Molecular Biology (ASBMB)

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          Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites.

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            A Nonribosomal System of Peptide Biosynthesis

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              An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein.

              A plasmid vector has been constructed that directs the synthesis of high levels (approximately 2% of total cellular protein) of fusions between a target protein and maltose-binding protein (MBP) in Escherichia coli. The MBP domain is used to purify the fusion protein in a one step procedure by affinity chromatography to crosslinked amylose resin. The fusion protein contains the recognition sequence (Ile-Glu-Gly-Arg) for blood coagulation factor Xa protease between the two domains. Cleavage by factor Xa separates the two domains and the target protein domain can then be purified away from the MBP domain by repeating the affinity chromatography step. A prokaryotic (beta-galactosidase) and a eukaryotic (paramyosin) protein have been successfully purified by this method.
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                Author and article information

                Journal
                Journal of Biological Chemistry
                J. Biol. Chem.
                American Society for Biochemistry & Molecular Biology (ASBMB)
                0021-9258
                1083-351X
                December 27 1996
                December 27 1996
                December 27 1996
                : 271
                : 52
                : 33225-33230
                Article
                10.1074/jbc.271.52.33225
                9a913455-dfd8-41cd-b707-f5727bb119cf
                © 1996
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