Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2008 Dec;1(2):147-52.
doi: 10.1161/CIRCGENETICS.108.811638.

Determination of paraoxonase 1 status without the use of toxic organophosphate substrates

Rebecca J Richter  1 , Gail P Jarvik, Clement E Furlong
Affiliations

Determination of paraoxonase 1 status without the use of toxic organophosphate substrates

Rebecca J Richter et al. Circ Cardiovasc Genet. 2008 Dec.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Structures of the substrates used for determining PON1 status.
Figure 2
Figure 2
Spectra of CMPA (●–●) and 4-(chloromethyl)phenol (○–○) and the difference spectrum (+–+).
Figure 3
Figure 3
Rates of hydrolysis of (A) PA by PON1Q192 (○–○) and PON1R192 (Δ–Δ); and (B) CMPA by PON1Q192 (○–○) and PON1R192 (Δ–Δ) as a function of sodium chloride concentration.
Figure 4
Figure 4
Substrate dependent rates of hydrolysis of (A) PA by PON1Q192, (B) PA by PON1R192, (C) CMPA by PON1Q192, and (D) CMPA by PON1R192. The assays for PA hydrolysis were run at high salt and those for CMPA at low salt as described in Methods section. Closed symbols indicate plots of velocity (v) versus substrate concentration [S]; open symbols, [S]/v versus [S].
Figure 5
Figure 5
Comparison of the 2 protocols for determining PON1 status. A, Assays using the highly toxic OP substrates DZO and PO. B, Assays using the non-OP substrates PA and CMPA. (○) indicates PON1Q/Q192;(■), PON1Q/R192;(Δ), PON1R/R192.
Figure 6
Figure 6
Rates of PA hydrolysis for each PON1192 phenotype/genotype at low salt concentration: PON1Q/Q192 (○–○), PON1Q/R192, (□–□) and PON1R/R192 (Δ–Δ). Horizontal bars represent the mean AREase activity values for each phenotype.
See this image and copyright information in PMC

Comment in

References

    1. Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN. The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996;33:498–507. - PubMed
    1. Mackness MI, Hallam SD, Peard T, Warner S, Walker CH. The separation of sheep and human serum “A”-esterase activity into the lipoprotein fraction by ultracentrifugation. Comp Biochem Physiol B. 1985;82:675–677. - PubMed
    1. Blatter MC, James RW, Messmer S, Barja F, Pometta D. Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase. Eur J Biochem. 1993;211:871–879. - PubMed
    1. Draganov DI, Stetson PL, Watson CE, Billecke SS, La Du BN. Rabbit serum paraoxonase 3 (PON3) is a high density lipoprotein-associated lactonase and protects low density lipoprotein against oxidation. J Biol Chem. 2000;275:33435–33442. - PubMed
    1. Reddy ST, Wadleigh DJ, Grijalva V, Ng C, Hama S, Gangopadhyay A, Shih DM, Lusis AJ, Navab M, Fogelman AM. Human paraoxonase-3 is an HDL-associated enzyme with biological activity similar to paraoxonase-1 protein but is not regulated by oxidized lipids. Arterioscler Thromb Vasc Biol. 2001;21:542–547. - PubMed

Publication types

Substances