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

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J. Lipid Res., doi:10.1194/jlr.M300464-JLR200
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Submitted on November 6, 2003
Revised on December 10, 2003
Accepted on December 17, 2003

Separation and quantitative recovery of mouse serum arylesterase and carboxylesterase activity by size-exclusion chromatography and ultracentrifugation

Philip W. Connelly, Graham F. Maguire, and Dragomir I. Draganov

J. Alick Little Lipid Research Laboratory, St. Michael's Hospital, Toronto, ON M5B 1A6

Corresponding Author: connellyp{at}smh.toronto.on.ca

Paraoxonase-1 (PON1) is known to be associated with high density lipoproteins. We optimized buffer conditions to obtain quantitative recovery of PON1 (arylesterase) activity and analysed the distribution of PON1 in mice using a combination of size-exclusion chromatography and ultracentrifugation. Size-exclusion chromatography of mouse serum separated the esterase activity into two peaks, one overlapping the high density lipoproteins and a second peak of lower molecular weight, consistent with serum carboxylesterase, that accounted for about 20% of the total esterase activity of normal mouse serum. Using conditions for the quantitative recovery of the arylesterase activity, we fractionated serum by ultracentrifugation into d < 1.21, d < 1.25, d > 1.21 and d > 1.25 g/ml fractions. We observed that PON1 arylesterase activity and mass were isolated in the d < 1.21 g/ml fraction and that serum carboxylesterase was recovered in the d > 1.25 g/ml fraction. The significance of the confounding of PON1 arylesterase activity by serum carboxylesterase was demonstrated by studying mice challenged with a high-fat, high cholate diet for 14 days. It was shown that all of the decrease in arylesterase activity in response to this diet is due to the HDL associated arylesterase activity (PON1). We conclude that mouse PON1 is quantitatively associated with high density lipoproteins. The contribution of serum carboxylesterase to the total esterase activity significantly confounds the interpretation of total arylesterase activity in mouse serum.


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