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Pediatric Hematology and Oncology, 2012 Paraoxonase-1 is an esterase enzyme and it has 3 types of activity, namely paraoxonase, arylesterase, and diazoxonase. It has been reported that paraoxonase-1 deficiency is related to increased susceptibility to development of atherosclerosis and ...
Hakim Çelik +2 more
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Clinical and Genetic Association of Serum Paraoxonase and Arylesterase Activities With Cardiovascular Risk [PDF]
Arteriosclerosis, Thrombosis, and Vascular Biology, 2012 Objective—Diminished serum paraoxonase and arylesterase activities (measures of paraoxonase-1 [PON-1] function) in humans have been linked to heightened systemic oxidative stress and atherosclerosis risk. The clinical prognostic use of measuring distinct
Stanley L. Hazen +2 more
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The activity of paraoxonase and arylesterase in patients with osteomyelitis
Scandinavian Journal of Clinical and Laboratory Investigation, 2012The aim of this study was to evaluate oxidative stress and to determine the activity of paraoxonase and arylesterase in patients with osteomyelitis compared to healthy controls.In total, 30 patients diagnosed with osteomyelitis and 30 healthy volunteers were enrolled in the study.
Suda Tekin Koruk
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Inhibition of arylesterase by aliphatic alcohols
Chemico-Biological Interactions, 1998The inhibition of arylesterase (EC 3.1.8.1) by 11 aliphatic alcohols (one to seven carbon atoms) was studied in blood serum from healthy donors. Inhibition curves were described by the Hill equation, with a Hill coefficient (n) close to unity, except for some alcohols, mainly the lowest.
Debord, J. +5 more
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Serum paraoxonase and arylesterase activities in patients with epithelial ovarian cancer
Gynecologic Oncology, 2009 Objective: The HDL-associated paraoxonase and arylesterase activities play a role in decreasing oxidative stress, which is known to contribute to cancer development.
Özcan Bektaş +2 more
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Continuous monitoring of arylesterase in human serum
Clinica Chimica Acta, 2001Arylesterase (EC 3.1.1.2) activity in serum was specifically measured using thiophenyl acetate in a mechanized assay at 37 degrees C with 4-bromophenylboronic acid as inhibitor of cholinesterase and hexacyanoferrate-III as indicator. The systematic development of a routine method, apparent limitations of thiophenyl compounds as arylesterase substrates,
K, Lorentz, W, Wirtz, T, Weiss
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Paraoxonase and arylesterase levels in rheumatoid arthritis
Clinical Rheumatology, 2006It was reported that lipid peroxidation (LPO) products increase in rheumatoid arthritis (RA) patients and increased LPO products reduce many antioxidants. Lipid hydroperoxides (LOOHs) are byproduct of LPO. Paraoxonase (PON), arylesterase (ARE), free sulfhydryl (SH) groups, and ceruloplasmin (CP) are enzymes or proteins with antioxidant characteristics.
A, Isik +4 more
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Arylesterases in blood: Effect of calcium and inhibitors
Biochemical Pharmacology, 1960Abstract (1) The normal functioning of human serum arylesterase requires the presence of calcium. An enzyme in human plasma fraction IV-I is probably identical with serum arylesterase. The activity of arylesterase is accelerated by calcium, inhibited by various chelating agents, metal ions, SH-reagents, and competitively and reversibly inhibited by ...
E G, ERDOS, C R, DEBAY, M P, WESTERMAN
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Serum arylesterase isoenzymes in chronic hepatitis
Clinical Biochemistry, 1974A new simple technique for the electrophoretic fractionation of arylesterase isoenzymes on cellulose acetate is described. Such a technique is a diagnostic tool in liver pathology insofar as it allows a differential evaluation of chronic aggressive hepatitis and persistent hepatitis.
Burlina, Angelo, Lauro, Galzigna
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Cholinesterase, arylesterase et proteinuries
Clinica Chimica Acta, 1974Resume A report is given on 80 cases of proteinuria and 60 sera provided by the same patients. The cholinesterase and arylesterase activities determined demonstrate that both enzymes pass in the urine at proportionally very low rates and the observed activities in urine are very different according to the individual cases.
D. Vincent, J. Magron
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