Serum Arylesterase Research Articles

Decreased Serum Paraoxonase-1 Activity during Intestinal Nematode (Nippostrongylus brasiliensis) Infection in Rats

Reduced paraoxonase-1 (PON1) activity has been observed in a number of pathological conditions; however, little is known about the effects of intestinal nematode infections, such as Nippostrongylus brasiliensis, on paraoxonase activity. We observed a significant reduction in serum paraoxonase and arylesterase activity after N. brasiliensis infection in Wistar rats from Day 6 until Day 12 post-infection (p.i.) for serum paraoxonase and from Day 3 until Day 24 p.i. for arylesterase. In addition, N. brasiliensis infection increased serum concentrations of pro-inflammatory cytokines (interleukin-1, interleukin-6, and tumor necrosis factor-alpha), with maximum concentrations observed on Day 9 p.i. These cytokines are known to inhibit the synthesis of hepatic PON1 mRNA. Thus, the observed reduction in PON1 activity during N. brasiliensis infection is likely associated with inflammatory reactions mounted against the parasites.

Arylesterase Activity and Antioxidant Status Depend on PON1-Q192R and PON1-L55M Polymorphisms in Subjects with Increased Risk of Cardiovascular Disease Consuming Walnut-Enriched Meat

Human paraoxonase (PON1) exists in 2 major polymorphic forms and has been shown to protect LDL and HDL against oxidation. The aim of this study was to assess the differences between subjects at increased risk of cardiovascular disease (CVD), taking into account the effects of PON1-Q192R and PON1-L55M polymorphisms on 1) basal serum arylesterase activity, lipid peroxidation (LPO), and LDL-cholesterol (LDL-C), HDL-C, total cholesterol (TC), and oxidized-LDL (ox-LDL) concentrations; 2) the relations between arylesterase activity and lipid variables; and 3) the effect of walnut-enriched meat (WM) consumption on arylesterase activity and lipid variables. Twenty-three Caucasians at increased risk of CVD were randomly assigned to diet order groups in a crossover, nonblinded, placebo-controlled trial, consisting of two 5-wk experimental periods [WM and control meat (CM)]. Significant PON1-L55M × PON1-Q192R interactions affected basal serum HDL-C (P = 0.019), LDL-C (P = 0.028) and TC (P = 0.022) and tended to affect arylesterase activity (P = 0.083). Basal arylesterase activity was positively correlated with basal HDL-C (r = 0.53; P < 0.05) and TC (r = 0.43; P < 0.05) and negatively correlated with LPO (r = −0.70; P < 0.01) and the ox-LDL:LDL ratio (r = −0.63; P < 0.01). WM decreased arylesterase activity in PON1-55M carriers (P = 0.012) but not in PON1-L55 individuals, and decreased LPO concentrations in PON1-192R carriers (P = 0.031) but not in PON1-Q192 subjects. To conclude, serum TC, HDL-C, and LDL-C concentrations and arylesterase activity depend on the interaction of PON1-L55M and PON1-Q192R polymorphisms. However, the PON1-Q192R polymorphism is more closely related to antioxidant status. Both polymorphisms modulate the effect of WM consumption on CVD biomarkers.

Paraoxonase and arylesterase activities in fibromyalgia

We aimed to evaluate the association of serum paraoxonase and arylesterase activities and oxidative/antioxidative status in patients with fibromyalgia. Forty-two patients with fibromyalgia and 53 healthy controls were included in the study. Serum paraoxonase and arylesterase activities were measured spectrophotometrically. Oxidative and antioxidative status were evaluated by measuring serum lipid hydroperoxide (LOOH) levels, total antioxidant status (TAS) and free sulfhydryl groups (–SH = total thiol). Lipid parameters were determined by routine laboratory methods. Serum paraoxonase and arylesterase activities, and TAS were lower in patients with fibromyalgia than in controls (P < 0.001, for all), and the –SH level was also lower in the patient group (P = 0.03). LOOH levels were higher in the patient group than in controls (P = 0.01). Our results suggest that patients with fibromyalgia were exposed to oxidative stress, and paraoxonase and arylesterase activities were decreased in these patients. Patients with fibromyalgia might be prone to development of atherosclerosis with reduced paraoxonase and arylesterase activities.

Correlation of serum arylesterase activity on phenylacetate estimated by the integrated method to common classical biochemical indexes of liver damage

The correlation of serum arylesterase (PON1) activity on phenylacetate determined by an integrated method to classical biochemical indexes of liver damage was investigated for the use of PON1 activity to evaluate liver damage. PON1 reaction curve as absorbance at 270 nm for 0.20 mmol/L phenylacetate hydrolysis was analyzed by the integrated method to determine maximal PON1 reaction rate. Classical biochemical indexes of liver damage were determined routinely. The 95% confidence threshold of PON1 activity in sera from healthy individuals was 2.12 mkat/L [(4.73+/-1.31) mkat/L, n=105]. PON1 activity in clinical sera was closely correlated to serum albumin, total protein and the ratio of albumin to globulins, but was weakly correlated to both direct and total bilirubin in serum. There were no correlations of PON1 activity to gamma-glutamyltransferase, alkaline phosphatase, alanine aminotransferase and aspartate aminotransferase. Among 127 clinical sera with PON1 activity>2.12 mkat/L, there were 92% healthy individuals examined by albumin, 90% healthy individuals examined by total protein, 88% healthy individuals examined by total bilirubin, 86% healthy individuals examined by direct bilirubin and 64% healthy individuals examined by the ratio of albumin to globulins, respectively. In each group of healthy individuals judged by classical biochemical indexes of close correlation to PON1 activity, percentage of healthy individuals examined by PON1 activity was always >80%. These results suggested PON1 activity on phenylacetate estimated by the integrated method was also suitable for the evaluation of liver damage.

Paraoxonase-1 activity as a marker of atherosclerosis is not associated with low bone mineral density in healthy postmenopausal women

The aging process is associated with an increasing prevalence of osteoporosis and atherosclerosis, but it is uncertain if these two conditions are interrelated. Serum paraoxonase-1 (PON1) is a high-density lipoprotein (HDL) associated enzyme that has been implicated in the pathogenesis of atherosclerosis. Our aims of the study were to investigate (1) serum paraoxonase and arylesterase activities and, lipid hydroperoxide (LOOH) levels in healthy postmenopausal women and (2) whether there were any associations between these enzyme activities and bone mineral density (BMD). A total of 97 generally healthy postmenopausal women were enrolled in the study. BMD was measured at lumbar spine (LS) and femoral neck (FN) with dual energy X-ray absorptiometry. Serum paraoxonase and arylesterase activities were measured spectrophotometrically. LOOH levels were measured by iodometric assay. In this population, 50 (51%) women had BMD T scores < -2.5 at the LS and/or FN defined as osteoporosis and 47 (49%) of them had normal BMDs. Serum paraoxonase, arylesterase, and LOOH activities were not significantly different between osteoporotic and nonosteoporotic postmenopausal women. There were also no correlations between paraoxonase, arylesterase, LOOH activities, and LS BMD and FN BMD. We conclude that there may be not good evidence to support a direct relationship between osteoporosis and atherosclerosis in these subjects. However, prospective studies with larger groups are needed to investigate this issue further.

Indications that paraoxonase-1 contributes to plasma high density lipoprotein levels in familial hypercholesterolemia

HDL-associated paraoxonase type 1 (PON1) can protect LDL and HDL against oxidative modification in vitro and therefore may protect against cardiovascular disease. We investigated the effects of PON1 levels, activity, and genetic variation on high density lipoprotein-cholesterol (HDL-C) levels, circulating oxidized LDL (OxLDL), subclinical inflammation [high-sensitive C-reactive protein (Hs-CRP)], and carotid atherosclerosis. PON1 genotypes (L55M, Q192R, -107C/T, -162A/G, -824G/A, and -907G/C) were determined in 302 patients with familial hypercholesterolemia. PON1 activity was monitored by the hydrolysis rate of paraoxon, diazoxon, and phenyl acetate. PON1 levels, OxLDL, and Hs-CRP were determined using an immunoassay. The genetic variants of PON1 that were associated with high levels and activity of the enzyme were associated with higher HDL-C levels (P values for trend: 0.008, 0.020, 0.042, and 0.037 for L55M, Q192R, -107C/T, and -907G/C, respectively). In addition to the PON1 genotype, there was also a positive correlation between PON1 levels and activity and HDL-C (PON1 levels: r = 0.37, P < 0.001; paraoxonase activity: r = 0.23, P = 0.01; diazoxonase activity: r = 0.29, P < 0.001; arylesterase activity: r = 0.19, P = 0.03). Our observations support the hypothesis that both PON1 levels and activity preserve HDL-C in plasma.

Serum arylesterase and paraoxonase activity in patients with chronic hepatitis

To investigate the relationship between serum paraoxonase (PON1), AST, ALT, GGT, and arylesterase (AE) activity alterations and the degree of liver damage in patients with chronic hepatitis. We studied 34 chronic hepatitis patients and 32 control subjects, aged between 35 and 65 years, in the Department of Infection and Clinical Microbiology at the Firat University School of Medicine. Blood samples were collected from subjects between 8:00 and 10:00 a.m. following a 12-h fast. Baseline and salt-stimulated PON1 activities were measured by the hydrolysis of paraoxon. Phenyl acetate was used as the substrate and formed phenol was measured spectrophotometrically at 270 nm after the addition of a 10-fold diluted serum sample in AE activity measurements. The results of this investigation revealed that the levels of AE activity decreased from 132+/-52 to 94+/-36 (29%), baseline PON1 activity from 452+/-112 to 164+/-67 (64%), salt-stimulated PON1 activity from 746+/-394 to 294+/-220 (61%), HDL from 58.4+/-5.1 to 47.2+/-5.6 (20%), triglyceride from 133+/-51.2 to 86+/-34.0 (35%), while a slight increase in the level of LDL (from 163+/-54.1 to 177.3+/-56.0; 9%) and significant increases in the levels of AST (from 29+/-9.3 to 98+/-44), ALP (from 57.2+/-13.1 to 91+/-38.1), ALT (from 27.9+/-3.32 to 89+/-19.1), GGT (from 24.3+/-2.10 to 94+/-48.2), total bilirubin (from 0.74+/-0.02 to 1.36+/-0.06; 84%) and direct bilirubin (from 0.18+/-0.01 to 0.42+/-0.04; 133%) were detected. However, the levels of albumin, total protein, cholesterol, and uric acid were almost the same in chronic hepatitis and the control subjects. Low PON1 and AE activity may contribute to the increased liver dysfunction in chronic hepatitis patients by reducing the ability of HDL to retard LDL oxidation and might be clinically useful for monitoring the disease of chronic hepatitis.

1252 Serum paraoxonase and arylesterase activities in alcohol-dependent patients

1252 Serum paraoxonase and arylesterase activities in alcohol-dependent patients

Associations between HDL oxidation and paraoxonase-1 and paraoxonase-1 gene polymorphisms in families affected by familial combined hyperlipidemia

It has been shown in vitro that the HDL-bound enzyme paraoxonase-1 (PON1) protects LDL against oxidation, and PON1 and PON1 gene polymorphisms may affect the oxidation of HDL particles. The aim of this study was to investigate the associations between in vitro HDL oxidation parameters, endogenous PON1 and PON1 genotypes in families affected by asymptomatic FCHL. Serum arylesterase (ARE) and PON1 activities, PON1 mass, PON1 genotypes and the kinetics of CuSO4-induced HDL oxidation in vitro were measured in 150 members of FCHL families free of clinical CAD. At univariate analysis, log PON1/apoA-I and the PON1 mass/apoA-I ratio significantly correlated with lag time, maximum diene formation and the propagation rate. The oxidation parameters also correlated with PON1 genotypes. Multivariate analysis showed that the associations between PON1 mass/unit apoA-I and the oxidation parameters were independent of the other variables. The lag time of HDL oxidation was also associated with the PON1 genotype 192QR. Endogenous PON1 may have protective effects on the different stages of HDL oxidation in the members of families affected by FCHL. This protective effect is independent of other biochemical factors, but may be influenced by the PON1 gene polymorphism. The endogenous PON1 content of HDL seems to be an important determinant of the anti-atherogenicity of this lipoprotein.

Separation and quantitative recovery of mouse serum arylesterase and carboxylesterase activity

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 analyzed 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, which accounted for approximately 20% of the total esterase activity of normal mouse serum. Using conditions for the quantitative recovery of arylesterase activity, we fractionated serum by ultracentrifugation into d < 1.21 g/ml, d < 1.25 g/ml, d > 1.21 g/ml, 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 attributable 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.

Levels of paraoxonase and arylesterase activities and malondialdehyde in workers exposed to ionizing radiation.

We examined levels of malondialdehyde (MDA) (an end-product of lipid peroxidation) and paraoxonase (PON1) (an antioxidant enzyme) activity and PON1 phenotypes in people who were exposed to ionizing radiation for different time periods and doses. A total of 78 individuals (mean age 34 +/- 7 years) were included in the study. Fifty-one of them were radiology workers whereas the control group was composed of 27 healthy volunteers who had never worked in a radiology-related job. Paraoxon was used as substrate for measurement of PON1 activity levels (basal and NaCl-stimulated). Phenylacetate was used as substrate for measurement of arylesterase activity levels. Cumulative levels of serum NaCl-stimulated PON1/arylesterase activities were utilized for phenotypic differentiation. In radiology workers, three different phenotypes were determined based on paraoxonase/arylesterase ratio. The ratios were 1.09 +/- 0.30 for AA (homozygote low activity); 2.91 +/- 1.07 for AB (heterozygote activity) and 4.97 +/- 1.21 for BB (homozygote high activity). There was a statistically meaningful negative correlation between serum MDA levels and PON1 activity levels in all phenotypes (p < 0.05). PON1 activity levels were found to be 25-35% lower in people who were exposed to long-term ( > 5 years) radiation compared to controls. There was no statistically significant correlation between serum arylesterase activity and MDA levels in these subjects (r = -0.185, p > 0.05). PON1 activity levels were decreased whereas serum MDA levels were increased in individuals exposed to radiation for a long period. PON phenotypes of people employed in jobs which expose them to radiation should be determined and based on these findings they should be advised to avoid risk factors inducing oxidative stress, such as smoking, and to consume foods rich in vitamins and trace elements to increase their antioxidant capacity.

Inhibition of human serum arylesterase by metal chlorides

The inhibition of arylesterase (paraoxonase, EC 3.1.8.1) by metal chlorides was studied with both pooled human serum (A phenotype) and purified enzyme, using phenyl acetate as substrate. Inhibition data were analysed with the Hill equation. Results obtained with whole serum and purified enzyme were very similar. On the basis of the Hill coefficient, n H, three groups of inhibitors were distinguished: (1) Cu 2+ and Hg 2+ for which n H=1, suggesting a single binding site (probably the free cysteine at position 283); these metals were mixed inhibitors, with more affinity for the free enzyme than for the enzyme–substrate complex; (2) Mn 2+, Co 2+, Ni 2+, Zn 2+, and Cd 2+ for which n H>1, suggesting several cooperative binding sites; (3) La 3+, for which n H<1. Within groups (1) and (2) the inhibiting potency followed the order of the periodic table. For the 3d elements the inhibiting order followed the Irving–Williams series, with the classical exception of Cu 2+. Only Zn 2+ was inhibitory at its physiological concentration.

Assay of serum arylesterase activity by fitting to the reaction curve with an integrated rate equation

Background: Conventional enzyme activities make use of the initial reaction rate at high substrate concentrations. Because this is not always practical, alternative enzyme assays have been sought. Methods: Reaction curve fitting with an integrated rate equation was investigated to assay serum arylesterase (ArE) activity using phenyl acetate (PA) and p-nitrophenol acetate (PNPA) as substrates. At a much lower initial concentration of substrate ( S 0), the simplified integrated rate equation for the ArE reaction was ln( S 0/ S i )=( V m/ K m+ K d) t i . Treating S 0 as a parameter, the enzyme activity as V m/ K m was estimated through nonlinear least square fitting to reaction curve, and the multiplication of V m/ K m by K m produced V m. Spontaneous hydrolysis of the substrate with a rate constant, K d, served as the background for the estimation of V m/ K m. Results: Substrate concentration at 8% of K m was well suited for the estimation of V m/ K m. With either substrate, the V m/ K m showed a close relation to the percentage of substrate consumed, and was not affected by common systematic errors. With either substrate, the between-run precision for V m/ K m was 6% ( n>7), V m/ K m was proportional to the amount of ArE and closely correlated with its initial rate. The upper limit of linearity by this integrated method was much higher than the initial rate method, while the detection limit was comparable. By using either V m/ K m or the initial rate, there was negligible interference with ArE activity assay from triglycerides, bilirubin, and hemoglobin. Conclusions: These results indicate the feasibility of the integrated method for routine assay of serum enzyme activity.

Gene Therapy to Prevent Organophosphate Intoxication

The specific hydrolytic activity of PON1 paraoxonase/arylesterase enzymes in liver and blood provides a natural barrier against the entry of organophosphate toxins into the central and peripheral nervous systems. Inherited differences in PON1 enzyme concentrations may determine levels of susceptibility to organophosphate injury in humans. To test whether boosting serum levels of PON1 enzymes by gene therapy might provide increased protection, we compared the degree of inactivation of whole brain acetylcholinesterase of mice exposed to chlorpyrifos 4 days after intravenous injection of recombinant adenoviruses containing PON1-LQ or PON1-LR genes or no PON1 gene. Both recombinant viruses containing PON1 genes boosted serum arylesterase concentrations by approximately 60% and significantly prevented the inactivation of brain acetylcholinesterase. Some mice were completely protected. These findings indicate that boosting serum levels of PON1 enzymes by a gene delivery vector raises the threshold for organophosphate toxicity by hydrolytic destruction before the chemical can enter the brain.

A sandwich enzyme-linked immunosorbent assay for human serum paraoxonase concentration

Serum paraoxonase (PON) is associated with plasma high density lipoproteins, and prevents the oxidative modification of low density lipoproteins. We have developed a sensitive sandwich enzyme-linked immunosorbent assay (ELISA), using two monoclonal antibodies against PON, to measure serum PON concentration. The concentration of PON in healthy Japanese subjects was 59.3 +/- 1.3 microgram/mL (mean +/- SEM; n = 87). Serum PON concentrations in relation to the PON 192 genetic polymorphism were: 69.5 +/- 2.9 microgram/mL in the QQ genotype; 63.0 +/- 1.9 microgram/mL in the QR genotype; and 52.8 +/- 1.7 microgram/mL in the RR genotype. Concentrations were significantly lower in the RR than in the QQ genotype (P < 0.01). Serum paraoxonase specific activity was higher in RR than in QQ subjects (18.6 +/- 0.40 vs. 2. 56 +/- 0.05 nmol/min/microgram, P < 0.01), but arylesterase specific activity was unrelated to genotype. PON concentration was positively associated (P < 0.001) with both serum arylesterase activity and, after adjusting for the effect of the position 192 polymorphism, with serum paraoxonase activity. Subjects with angiographically verified coronary heart disease had significantly lower PON concentrations than the healthy controls (52.0 +/- 2.3 microgram/mL; n = 35, P < 0.01). This association was independent of the position 192 genotype. Our new ELISA should be of value for epidemiologic and clinical studies of serum PON concentration. immunosorbent assay for human serum paraoxonase concentration.

Age related decrease of high density lipoproteins (HDL) in women after menopause. Quantification of HDL with genetically determined HDL arylesterase in women with healthy coronary vessels and in women with angiographically verified coronary heart disease

The decline in the concentration of high density lipoproteins (HDL) observed in postmenopausal women is thought to contribute to the increasing incidence of coronary artery disease (CAD) after menopause. Human serum arylesterase (EC 3.1.1.2) is exclusively associated with HDL. We therefore investigated possible differences in the decline of HDL-levels and of HDL-subfractions HDL2 and HDL3 between postmenopausal women without and with angiographically documented CAD. HDL-, HDL2-and-HDL3- concentrations were studied in postmenopausal women with angiographically documented CAD (n = 24; 51 to 72 years mean: 62 years) and compared to HDL-parameters of women without CAD (n = 22; 51 to 81 years, mean: 58 years). Arylesterase activities of HDL2-and HDL3-subfractions and HDL2-cholesterol concentrations were determined after differential precipitation with polyethylene glycol (4.7 mM PEG). Phenotyping of HDL-arylesterase was achieved in CAD patients and in women without CAD after determining hydrolysis of arylesterase substrates paraoxon (PO) and phenylacetate (PA) by calculating paraoxonase/arylesterase activity ratios R (R = [PO]/[PA] x 1000): phenotype A (n = 26) with R < 2.5, phenotype AB (n = 16) with 5.0 < R < 10.7, and phenotype B (n = 4) with R > 13.5. In postmenopausal women with documented CAD, as compared to women without CAD, HDL-cholesterol (55 +/- 3 mg/dl vs. 69 +/- 3 mg/dl HDL2-arylesterase (25 +/- 1 kU/l vs. 33 +/- 2 kU/l), and HDL3-arylesterase (89 +/- 4 kU/l vs. 106 +/- 5 kU/I) were found to be significantly reduced. Analysis of the correlation of lipid parameters and age revealed in CAD patients, but not in postmenopausal women without CAD, a significant increase of total cholesterol (r = 0.42), and significant reductions of both HDL2-arylesterase (r = -0.47) and HDL3-arylesterase (r = 0.74) with increasing age. In contrast, HDL-cholesterol (r = -0.14) and HDL2-cholesterol (r = -0.06) of CAD patients showed only slight and non-significant reductions with age. Since HDL3-arylesterase was found to be age-dependently reduced in women without CAD (r = 0.17), HDL2-arylesterase of postmenopausal women, among all lipid parameters showed the most pronounced differences between women without CAD and CAD patients. The age-dependent decrease of HDL2-arylesterase in postmenopausal women with CAD does not result from an increased frequency of B-allele carriers in the subgroup of CAD patients with an age above the median (64 years). Genetically determined serum HDL-arylesterase is well suited to quantify HDL in postmenopausal women without and with CAD. HDL2-arylesterase of postmenopausal women should be evaluated as a screening parameter for both primary and secondary CAD prevention.

Variation in serum arylesterase, β-glucuronidase, cathepsin L and plasminogen activators during pregnancy

To determine whether the activities of certain hydrolases (arylesterase, β-glucuronidase, cathepsin L, plasminogen activators, arginase, glutaminase, asparaginase and adenosine deaminase) are changed during pregnancy, three groups of 15 apparently healthy women (aged 18–38 years) in their first, second and third trimester of pregnancy were compared to a control group formed of 15 non-pregnant women of similar ages. Enzyme and specific activities gradually increased from the first to the end of the third trimester of pregnancy for arylesterase and β-glucuronidase, these increases being statistically significant ( P < 0.01) in comparison to controls. However, as regards cathepsin L and plasminogen activators, the greatest increase was found in the second trimester. Arginase, glutaminase and asparaginase activities were very low and not distinguishable from the controls. In conclusion, differences in the activities of several hydrolases have been found in the sera of healthy pregnant women in comparison to controls.

Association on red cell X-protein, NADH-diaphorase 1, malic enzyme and serum arylesterase phenotypes with economic traits in sheep

Association on red cell X-protein, NADH-diaphorase 1, malic enzyme and serum arylesterase phenotypes with economic traits in sheep

Molecular weight and substrate characteristics of human serum arylesterase following purification by immuno-affinity chromatography

Human serum arylesterase (EC 3.1.1.2) was purified over 400-fold with a recovery of 61–78% by single-step immuno-affinity chromatography using a monoclonal antiboddy, 12-1H8, as the adsorbent. The resultant preparation behaved as one component on SDS-PAGE with an apparent M r of 46,000, indicating its high homogeneity: Molecular weight was determined as 380,000 Da by HPLC on TSK-gel G-3000SW. The arylesterase molecule would thus appear to be comprised of octameric subunits. The purified protein hydrolyzed paraoxon. The present study suggests that a separate classification of EC 3.1.8.1 for its paraoxon hydrolyzing activity may not be appropriate to differentiate from arylesterase activity. In addition, the substrate for arylesterase is discussed in terms of its chemical structure.

Interindividual variations in enzymes controlling organophosphate toxicity in man.

1 Interindividual variations in an unexposed population have been defined for five enzymes involved in organophosphate (OP) toxicity. The enzymes measured were: red blood cell acetylcholinesterase (AChE), lymphocyte neuropathy target esterase (NTE), serum cholinesterase (ChE), serum paraoxonase and serum arylesterase. 2 AChE and arylesterase were normally distributed in the population whilst the distribution of NTE, ChE and paraoxonase deviated significantly from normal. 3 Assay precision and intra-individual variability were measured for each of the enzymes; the effect on interindividual variation was assessed. 4 Variations in enzyme activities between individuals could have profound effects on susceptibility to OP toxicity. Prior determination of these enzymes may be predictive of susceptibility. 5 Lymphocyte NTE has some limitations as an indicator of exposure to neurotoxic OPs.