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At least 451 records · Page 25Linked to original sources
PubMed1983

[Effect of clofibrate on intracellular enzyme distribution in the rat liver].

The effect of chronic administration of a hypolipaemic agent--clofibrate--on the subcellular distribution of liver enzymes in male rats was studied. Clofibrate produced an increase in the number of peroxisomes and also enhanced the activity of aconitase and histidine: glyoxylate aminotransferase (HGA) in liver homogenate. Differential centrifugation of homogenate revealed an elevation of the relative amounts of catalase, HGA and isocitrate dehydrogenase in the soluble cell fraction in clofibrate pretreated animals. Clofibrate induced peroxisomal HGA but failed to alter the amounts of catalase, urate oxidase and isocitrate dehydrogenase in the particles. In both the experimental and control groups the activity of aconitase, malate dehydrogenase (NAD+), creatine phosphokinase and glutathione reductase was observed in mitochondrial fractions and was not detected in purified peroxisomes.

Animals↗
PubMed1995

[Alteration of peroxisomal enzyme activities in the liver of guinea pigs caused by coplanar PCB].

The hyperlipidemia is a well-known typical symptom in Yusho patients and experimental animals treated with PCBs. We have found a significant induction of CYP4A1, which catalyzes omega-hydroxylation of fatty acids, in guinea pigs by the treatment with a coplanar PCB, 3, 4, 5, 3',4-pentachlorobiphenyl (PenCB), though the P450 is reduced in the treated rats. Peroxisome has beta-oxidation enzymes distinct from mitochondrial enzymes, and also play an important role in lipid metabolism. Peroxisome proliferators have been shown to regulate the expression of CYP4A1 and peroxisomal enzymes by the same mechanism in the rat. In the present study, we examine the effect of PenCB treatment on peroxisomal enzymes in the liver of guinea pigs. As a result, the enzyme activities of hepatic peroxisome, e.g. fatty acid oxidizing system, catalase and urate oxidase, had a rising tendency by the treatment with PenCB in the animal. The results suggest that the regulation of peroxisomal enzymes and CYP4A1 is also associated in guinea pigs, and PenCB provides a similar effect of peroxisomal proliferators to the animal. The possible toxicity through the peroxisomal alteration was discussed.

Animals↗
PubMed1994

[A rare cause of hyponatremia during introductory treatment of acute lymphoblastic leukemia in an infant: inappropriate secretion of atrial natriuretic factor?].

BACKGROUND: --Hyponatremia is frequently seen during the treatment of acute lymphoblastic leukemia: its causes are numerous. This work aims to present a case in whom hyponatremia was possibly due to an increased secretion of atrial natriuretic factor. CASE REPORT: --A 3 week-old baby was admitted because of malignant hemopathy. A diagnosis of acute lymphoblastic leukemia was rapidly made and the patient was firstly given alkaline diuresis, urate-oxidase and corticosteroids. Vincristine and daunorubicin were associated one week later. Insertion of a central intravenous line in the right subclavicular artery failed so that this catheter was finally inserted into the left jugular vein. Natremia was 126 mmol/l at that time and dramatically decreased within 24 hours to 109 mmol/l without net changes in water and electrolytic input. At that time, sodium urinary excretion was 6 mmol/kg/day (diuresis: 420 mlF/day). There was no hemodynamic changes, nor digestive or cardiac manifestations. Ultrasonography showed that the left superior cava vein drained into the right cardiac atrium. The catheter was withdrawn and the patient was given sodium supplementation permitting complete and definitive cure of hyponatremia within 2 days. CONCLUSIONS: --All usual causes of hyponatremia having been ruled out in this patient, we postulate that hyponatremia was due to direct stimulation of atrial natriuretic peptide through an increase in atrial pressure secondary to the catheter insertion near the cardiac atrium.

Atrial Natriuretic Factor↗
PubMed1994

[Hyperuricemia and gout: therapeutic indications].

Uricaemia-lowering treatment is indicated when hyperuricaemia is pronounced (90 mg/L or more) or when it is expressed by uric acid stones and/or gout. The drugs which lower plasma uric acid levels are presented according to their mode of action: uric acid inhibitors (allopurinol and tisopurine), uric acid excretors (probenecid, benzbromarone) and the uric acid lyser (urate-oxidase). The pharmacological and pharmaceutical data needed to understand the respective indications and applications of these drugs are given. These indications and those of adjuvant therapies are presented as answers to the following questions: when should a uricaemia-lowering treatment be initiated? What are the general rules to be obeyed? Which indications or contraindications must be borne in mind?

Acute Disease↗
PubMed1998

Exploring hydrophobic sites in proteins with xenon or krypton.

X-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures. These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination.

Animals↗
PubMed1979

Use of immobilized enzymes in automated clinical analysis: determination of uric acid and glucose using immobilized enzymes in column form.

We studied the use of immobilized enzymes, covalently bound to alkylaminosilane derivative of porous glass, to automated clinical analysis on uric acid and glucose in blood, serum and urine. A microcolumn with an immobilized enzyme was prepared and used in an AutoAnalyzer I continuous flow system. Uricase (EC 1.7.3.3) from Candida utilis and glucose oxidase (EC 1.1.3.4) from Aspergillus niger were immobilized for the determination of uric acid and glucose, respectively. Hydrogen peroxide produced by these oxidases was colorimetrically determined using horse-radish peroxidase (EC 1.11.1.7) and a hydrogen acceptor in solution. Sensitivity and wash charactertistics of a column with immobilized enzyme, 1.5 mm of inner diameter and up to 40 mm in length, were satisfactory at an assay speed of 50 samples per hour. The results correlated well with those obtained by other well established methods utilizing the AutoAnalyzer system. The immobilized enzymes were sufficiently stable for at least two months of 2000 tests when used repeatedly. Clinical trials proved that this method is capable of replacing the soluble enzyme method, giving reliable and reproducible results at lower cost.

Autoanalysis↗
PubMed1979

The use of immobilized enzyme reactors in continuous-flow analyzers for the determination of glucose, urea, and uric acid.

We describe the use of immobilized enzymes in assay methods for the determination of glucose with glucose oxidase, uric acid with uricase, and urea with urease in serum samples. The enzyme reactor tubes were adapted to continuous-flow analyzers (Technicon AA II, SMA 12/60, and SMAC) used in routine laboratory determinations, and results with their use were compared to those from assays involving soluble enzymes. We substituted the reactors for the free enzyme reagents in the respective channels of the SMA 12/60 and SMAC, without modifying the parameters of the remaining channels. We compared assay sensitivity, precision, and carryover for immobilized and conventional liquid enzymes. Immobilized enzyme reactors provide accurate, reliable, convenient, and economical alternatives to the use of free enzyme reagents in these systems.

Autoanalysis↗
PubMed1978

[Changes in peroxidation under conditions of 3,4-benzypyrene-induced carcinogenesis].

The activities of enzymatic systems generating and destroying peroxides and the lipid peroxide content in neoplastic rat liver and 3,4-benzpyrene-induced sarcoma were studied. The tumour was characterized by high activity of glutathione peroxidase and low activity of catalase. No urate- and glycolate oxidases or ascorbat dependent peroxidation of lipids and lipid peroxides were found in the tumour. In the liver of neoplastic animals the activities of glutathione peroxidase and NADPH-dependent system of microsomal phospholipid peroxidation and the lipd peroxides content were increased, whereas the activities of catalase and urate oxidase were decreased.

Alcohol Oxidoreductases↗