Human serum paraoxonase

K. N. Gan, A. Smolen, H. W. Eckerson, B. N. La Du, Purification of Human Serum Paraoxonase/Arylesterase. Evidence for One Esterase Catalyzing Both Activities , Drug Metab. Dispos. 1991,19, 100-106. 

N. La Du, The Human Serum Paraoxonase/Arylesterase Gene (PON1) Is One Member of a Multigene Family , Genomics 1996, 33, 498-507. 

Of great interest is the recent finding that human serum paraoxonase (EC 3.1.8.1, which belongs to the class of A-esterases), is very active in hydrolyzing a range of four-, five-, six-, and seven-membered lactones [167], Some cyclic carbonates (see Sect. 7.6.3) were also substrates. 

S. Billecke, D. Draganov, R. Councell, P. Stetson, C. Watson, C. Hsu, B. N. La Du, Human Serum Paraoxonase (PON1) Isozymes Q and R Hydrolyze Lactones and Cyclic Carbonate Esters , Drug Metab. Dispos. 2000, 28, 1335- 1347. 

T. L. Diepgen, M. Geldmacher-von Mallinckrodt, Interethnic Differences in the Detoxification of Organophosphates The Human Serum Paraoxonase Polymorphism , Arch. Toxicol. 1986, Suppl. 9, 154-158. 

Gan, K.N., et al. 1991. Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab Dispos 19 100. 

Mackness B, Mackness MI, Arrol S, Turkie W, Durrington PN. Effect of the human serum paraoxonase 55 and 192 genetic polymorphisms on the protection by high density lipoprotein against low density lipoprotein oxidative modification. FEB Lett 1998 423 57-60. 

Josse, D., Xie, W., Masson, P., Lockridge, O. (1999a). Human serum paraoxonase (PONl) identification of essential amino acid residues by group-selective labelling and site-directed mutagenesis. Chem. Biol. Interact. 119-20 71-8. 

Mackness, B., Durrington, P.N., Mackness, M.I. (1998a). Human serum paraoxonase. Gen. Pharmacol. 31 329-36. 

Primo-Parmo, S.L., Sorenson, R.C., Teiher, J., La Du, B.N. (1996). The human serum paraoxonase/arylesterase gene (PONl) is one member of a multigene family. Genomics 33 498-507. 

Yermg, D.T., Lenz, D.E., Cerasoli, D.M. (2005). Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates. FEBS J. Til 2225-30. 

Billecke, S., Draganov, D., Counsell, R., Stetson, P., Watson, C., Hsu, C., La Du, B.N. (2000). Human serum paraoxonase (PONl) isozymes Q and R hydrolyze lactones and cyclic carbonate esters. Drug Metab. Dispos. 28 1335-42. 

Davies, H.G., Richter, R.J., Keifer, M., Broomfield, C.A., Sowalla, J., Furlong, C.E. (1996). The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat. Genet. 14 334-6. 

Furlong, C.E. (2000). PONl status and neurologic symptom complexes in Gulf War veterans. Genome Res. 10 153-5. Furlong, C.E., Richter, R.J, Chapline, C., Crahh, J.W. (1991). Purification of rabbit and human serum paraoxonase. Biochemistry 30 10133-40. 

Geldmacher von Mallinckrodt, M., Diepgen, T.L. (1988). The human serum paraoxonase polymorphisms and specificity. Toxicol. Environ. Chem. 18 79-196. 

Leviev, I., Deakin, S., James, R.W. (2001). Decreased stability of the M54 isoform of paraoxonase as a contrihutory factor to variations in human serum paraoxonase concentrations. J. Lipid Res. 42 528-35. 

Sorenson, R.C., Bisgaier, C.L., Aviram, M., Hsu, C., Billecke, S., LaDu, B.N. (1999). Human serum paraoxonase/arylesterase s retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids apoprotein A-1 stabilizes activity. Arterioscler. Thromb. Vase. Biol. 19 2214-25. 

Structure/function analyses of human serum paraoxonase (HuPONl) mutants designed from a DFPase-like homology model. Biochim. Biophys. Acta 1702 (sl-11. 

Akgur SA, Ozturk R Solak I, Moral AR, Ege B. Human serum paraoxonase (PONl) activity in acute organophosphorus insecticide poisoning. Forensic Sci Int 2003 133 136-40. Garcia-Repetto R, Gimenez MP, Repetto M. New method for determination of ten pesticides in human blood. J AOAC Int 2001 84 342-9. 

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