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Cloning, purification, and refolding of human paraoxonase-3 expressed in Escherichia coli and its characterization.

Abstract：

:Human paraoxonase (hPON3) is a high density lipoprotein-related glycoprotein with multi-enzymatic properties and antioxidant activity which is proposed to participate in the prevention of low density lipoprotein (LDL) oxidation. In this study, hPON3 gene was amplified from Human Fetal Liver Marathon-Ready cDNA and expressed in Escherichia coli. A majority of the expressed protein existed as inclusion bodies. The inclusion bodies were solubilized with Triton X-100 and refolded in vitro. The refolded rhPON3 was purified by DEAE-Sepharose Fast Flow and its purity was up to 90%. The Km and Vmax values of refolded rhPON3, in respect to phenylacetate hydrolysis were 7.47 +/- 2.14 mM and 66 +/- 17 U/min/mg (n = 3). The Km and Vmax values of refolded rhPON3, in respect to dihydrocoumarin hydrolysis were 0.83 +/- 0.21 mM and 621 +/- 66 U/min/mg (n = 3). The refolded rhPON3 exhibited similar antioxidant activity to that of rhPON3 purified from the soluble fraction of cell lysate and could effectively protect LDL from Cu2+ induced oxidation.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Lu H,Zhu J,Zang Y,Ze Y,Qin J

doi

10.1016/j.pep.2005.07.021

keywords:

subject

Has Abstract

pub_date

2006-03-01 00:00:00

pages

92-9

issue

1

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(05)00258-5

journal_volume

46

pub_type

杂志文章

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