2011China BrewingRequires access

Cloning,expression and purification of rabbit serum paraoxonase in Escherichia coli

Jianyun Zhang

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Abstract

The paraoxonase gene PON1 was cloned from rabbit liver by RT-PCR,and cloned into PET32a vector and constructed the PET32a-PON1 recombinant plasmid.wased into component cells of and the Expression strain was obtained by transformation of PET32a-PON1 plasmid into E.coli.SDS-PAGE analysis revealed that the recombinant proteins could be partially soluble.Enzyme assay indicated that the recombinant proteins had arylesterase and lactonase activities.The results made a good base for studying the functions of purified PON1.

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What this paper is about

The paraoxonase gene PON1 was cloned from rabbit liver by RT-PCR,and cloned into PET32a vector and constructed the PET32a-PON1 recombinant plasmid.wased into component cells of and the Expression strain was obtained by transformation of PET32a-PON1 plasmid into E.coli.SDS-PAGE analysis revealed that the recombinant proteins could be partially soluble.Enzyme assay indicated that the recombinant proteins had arylesterase and lactonase activities.The results made a good base for studying the functions of purified PON1.

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Available abstract

The paraoxonase gene PON1 was cloned from rabbit liver by RT-PCR,and cloned into PET32a vector and constructed the PET32a-PON1 recombinant plasmid.wased into component cells of and the Expression strain was obtained by transformation of PET32a-PON1 plasmid into E.coli.SDS-PAGE analysis revealed that the recombinant proteins could be partially soluble.Enzyme assay indicated that the recombinant proteins had arylesterase and lactonase activities.The results made a good base for studying the functions of purified PON1.

Key concepts: Recombinant DNA, Paraoxonase, PON1, Escherichia coli, Arylesterase, Plasmid, Molecular biology, Cloning (programming)

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