J. Lipid Res.
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A more recent version of this article appeared on December 1, 2004

Papers In Press, published online ahead of print September 1, 2004
J. Lipid Res., doi:10.1194/jlr.M400213-JLR200
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Submitted on June 8, 2004
Revised on August 23, 2004
Accepted on August 24, 2004

Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH

John F. Teiber, Dragomir I. Draganov, and Bert N. La Du

Pharmacology Dept., The University of Michigan, Ann Arbor, MI 48109-0632

Corresponding Author: bladu{at}umich.edu

Purified serum PON1 had been shown to attenuate the oxidation of LDL in vitro. We critically re-evaluated the antioxidant properties of serum PON1 in the in vitro assays initiated with copper or the free radical generator 2, 2’-azobis-2-amidinopropane hydrochloride. The antioxidant activity of different purified PON1 preparations did not correlate with their arylesterase, lactonase or phopholipase A-2 activities, or with the amounts of detergent or protein. Dialysis of three of these preparations resulted in a 30-40 % loss of their arylesterase activities but in a complete loss of their antioxidant activities. We also followed the distribution of the antioxidant activity during human serum PON1 purification by two purification methods. The antioxidant activity of the anion exchange chromatography fractions did not co-purify with PON1 using either method and could largely be accounted for by the “antioxidant” activity of the detergent present. In conclusion, using the copper or AAPH in vitro assays no PON1-mediated antioxidant activity was detected suggesting that the removal of PON1 from its natural environment may impair its antioxidative activity and that this assay with highly purified PON1 may be an inappropriate method to study the antioxidative properties of the enzyme.


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