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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
7
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pubmed:dateCreated |
2005-9-12
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pubmed:abstractText |
Human paraoxnase-3 (hPON3) (EC3.1.8.1) is a lipid-associated enzyme with antioxidant activity, and can inhibit the oxidation of low-density lipoprotein (LDL), thereby inhibiting early atherogenic process. In the present study, human PON3 gene was cloned from Human Fetal Liver Marathon-Ready cDNA and expressed in insect cells using baculovirus vector. Twenty-eight milligrams of purified recombinant hPON3 (rhPON3) was obtained from 1L Sf9 cells culture. The Km and Vmax values of rhPON3, with respective to phenylacetate hydrolysis were 7.46+/-4.40 mM and 89+/-10.54 U/mg (n=3). The kinetic parameters of Vmax and Km for dihydrocoumarin hydrolysis by rhPON3 were 698+/-248 U/mg and 0.84+/-0.24 mM (n=3). LDL oxidation assay indicated that rhPON3 could effectively protect LDL against copper-induced oxidation in vitro.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2952
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1019-25
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16099434-Animals,
pubmed-meshheading:16099434-Aryldialkylphosphatase,
pubmed-meshheading:16099434-Baculoviridae,
pubmed-meshheading:16099434-Base Sequence,
pubmed-meshheading:16099434-Carboxylic Ester Hydrolases,
pubmed-meshheading:16099434-Cell Line,
pubmed-meshheading:16099434-Cloning, Molecular,
pubmed-meshheading:16099434-DNA Primers,
pubmed-meshheading:16099434-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:16099434-Esterases,
pubmed-meshheading:16099434-Humans,
pubmed-meshheading:16099434-Kinetics,
pubmed-meshheading:16099434-Oxidation-Reduction,
pubmed-meshheading:16099434-Recombinant Proteins,
pubmed-meshheading:16099434-Spodoptera
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pubmed:year |
2005
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pubmed:articleTitle |
Cloning, high level expression of human paraoxonase-3 in Sf9 cells and pharmacological characterization of its product.
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pubmed:affiliation |
School of Life Science and State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, People's Republic of China.
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pubmed:publicationType |
Journal Article
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