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[An artificial gene, biosynthesis and properties of the recombinant Fc fragment of human immunoglobulin G1].

Efimov Va, Kalinkina Al, Fradkov Af, Chakhmakhcheva Og

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Abstract

Chemicoenzymatic synthesis and cloning of a gene encoding the Fc domain of human immunoglobulin G1 were carried out. The artificial gene was expressed in Escherichia coli cells in plasmid vectors under control of a late T7 promoter. The recombinant protein isolated from the bacterial cells is capable of forming dimers and binding protein A from Staphylococcus aureus.

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Chemicoenzymatic synthesis and cloning of a gene encoding the Fc domain of human immunoglobulin G1 were carried out. The artificial gene was expressed in Escherichia coli cells in plasmid vectors under control of a late T7 promoter. The recombinant protein isolated from the bacterial cells is capable of forming dimers and binding protein A from Staphylococcus aureus.

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Available abstract

Chemicoenzymatic synthesis and cloning of a gene encoding the Fc domain of human immunoglobulin G1 were carried out. The artificial gene was expressed in Escherichia coli cells in plasmid vectors under control of a late T7 promoter. The recombinant protein isolated from the bacterial cells is capable of forming dimers and binding protein A from Staphylococcus aureus.

Key concepts: Recombinant DNA, Escherichia coli, Cloning (programming), Plasmid, Chemistry, Gene, Antibody, Molecular biology

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[An artificial gene, biosynthesis and properties of the recombinant Fc fragment of human immunoglobulin G1]. — Research Paper | ScholarLens