Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new enzymatic method for the determination of serum pseudo-cholinesterase activity is described. Choline, which is liberated from benzoylcholine as substrate by cholinesterase, is oxidized by choline oxidase to betaine with the simultaneous production of hydrogen peroxide, which oxidatively couples with 4-aminoantipyrine and phenol in the presence of peroxidase to yield a chromogen with maximal absorbance at 500 nm. The calibration curve is linear up to 1500 units per liter of serum. The method is reproducible, and the results correlate well with those obtained by the method using butyrylthiocholine as substrate and 5,5'-dithiobis-(2-nitrobenzoic acid) as color reagent.
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PMID:New enzymatic assay of cholinesterase activity. 2 Feb 53

Most of the currently used enzyme-immunological tests employ horse radish peroxidase as a marker enzyme. A new method is described for the determination of extremely small quantities of peroxidase. This largely prevents the inactivation of the peroxidase by H2O2 and thereby permits a much longer incubation time. In the presence of 25 mmol/l phenol, 2 mmol/l 4-amino-antipyrin and 0.8 mmol/l H2O2, peroxidase catalyses the formation of a red quinonimine, whose increase in adsorption is directly proportional to the enzyme concentration.
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PMID:[Enzyme-immunological tests: determination of the activity of peroxidase with the aid of the "Trinder reagent" (author's transl)]. 2 80

The localisation of lipopolysaccharide-binding sites on erythrocytes with peroxidase-coupled LPS is described. LPS was isolated from Fusobacterium nucleatum (Fus MC-8) by phenol-water extraction. The LPS was coupled to horseradish peroxidase by the two-step method of Avrameas and Ternynck (1971). The biological and serological activities of the conjugated LPS were compared with those of the native material. Peroxidase could be coupled to LPS without significant loss of endotoxic or serological activity. The LPS-peroxidase conjugate could be demonstrated on erythrocytes by light and electron microscopy.
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PMID:Ultrastructural localisation of lipopolysaccharide-binding sites with peroxidase-conjugated lipopolysaccharides. 10 40

The marine bacteria Beneckea harveyi and Photobacterium leiognathi were shown to bear mannose-containing binding sites for the mannosephilic lectins of Pseudomonas aeruginosa and concanavalin A (Con A). The interaction between the lectins and the marine bacteria was demonstrated by the bacteriagglutination test, by adsorption of the lectins onto the bacteria and by mannose-specific peroxidase-binding to the lectin-coated bacteria. Treatment of the bacteria with formaldehyde, phenol, ethanol or boiling them for 15 min, did not alter their ability to adsorb the lectins. The growth rate of the marine bacteria was unaffected when either the Pseudomonas lectins or Con A was added to the culture medium.
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PMID:Interaction of the mannosephilic lectins of Pseudomonas aeruginosa with luminous species of marine enterobacteria. 12 Sep 27

The activity of cytochrome oxidase in tissues was decreased in short-term adaptation to reduce pO2 and administration of KCN in small doses. In the former case the activities of peroxidase and catalase were increased in blood. These effects as well as administration of Na2ATP into rats led to an increase in water content in tissues, to soption of acidic vital stain (phenol red) and to decrease in the ether-soluble fraction of lipids. The alterations were accompanied by decreased permeability of cells to n-hexane (estimation by gas-liquid chromatography). The decrease in cell permeability for nonelectrolytes was apparently due to conformational alterations in protein molecule of cytoplasmic membranes.
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PMID:[Hypoxia and tissue permeability for non-electrolytes]. 19 82

A kinetic method for quantitation of peroxidase activity ('myeloperoxidase', E.C. 1.11.1.7.) in human granulocytes has been evaluated. The enzymic activity was determined at 37 degrees C, PH = 7.0. Substrates: 2-methyxo-phenol (1.25 mmol/l) and H2O2 (0.1 mmol/l). When applied on granulocytes from solitary blood samples from healthy, normal subjects the detected peroxidase activity varied considerably from one person to another (CV = 40-50%). Sequential determinations of the peroxidase activity in granulocytes from selected healthy, normal subjects demonstrated substantial intra-individual variations. Analysis of variance confirmed that the intra-individual variations (CV = 36%) exceeded all other variance components involved.
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PMID:Peroxidase activity in human granulocytes, inter- and intra-individual variations. 21 Apr 89

Estradiol 17 beta prevented the fall in the microbicidal activity of the myeloperoxidase-H2O2-halide system induced by high H2O2 concentrations. In contrast, when the H2O2 (and halide) concentrations were low the myeloperoxidase-H2O2-halide antimicrobial system was inhibited by estradiol. These properties of estradiol 17 beta were shared by estradiol 17 alpha, estrone, estriol, ethinyl estradiol, and phenol, but not by estradiol-3-benzoate, testosterone, progesterone, hydroxyprogesterone, cortisone, hydrocortisone, or deoxycorticosterone.
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PMID:Effect of estrogens on the myeloperoxidase-mediated antimicrobial system. 22 68

Manual procedures for estimating serum total cholesterol by use of cholesterol oxidase (EC 1.1.3.6) and the phenol--aminophenazone--peroxidase chromogenic system are described, in which cholesteryl esters are hydrolyzed either by use of pancreatic cholesterol ester hydrolase (EC 3.1.1.13) or saponification by ethanolic potassium hydroxide. Both methods are linear up to a cholesterol concentration of 12 mmol/L and are reproducible (between-run CV, about 1.1%). The chemical hydrolysis method yields results that are about 10% lower than those obtained by enzymic hydrolysis, because of incomplete removal of interfering thiols generated during the saponification of serum. The chemical hydrolysis procedure is much less susceptible to interferences, particularly by bilirubin, but the enzymic hydrolysis system is simpler to perform and therefore has a greater potential for mechanization.
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PMID:Enzymic assay of total cholesterol involving chemical or enzymic hydrolysis--a comparison of methods. 44 34

We evaluated the analytical performance of Trinder's glucose oxidase (EC 1.1.3.4)/peroxidase (EC 1.11.1.7) 4-aminophenazone-phenol method for the quantification of serum glucose as adapted to the Technicon SMAC. Our results correlated well with those by the routine SMAC glucose oxidase/peroxidase 3-methyl-2-benzothiazolinone hydrazone-N,N-dimethylaniline method (y = 1.02x - 49.4; r = 0.99) and the glucose oxidase oxygen-rate method (y = 0.99x + 14; r = 0.99) with the Beckman Glucose Analyzer. Sample-to-sample interaction was less than 1%. Ascorbic acid or uric acid in concentrations as high as 200 mg/L were without demonstrable effect on results for glucose. Intra- and inter-assay precisions (CV) were 1.6 and 2.3%, respectively. The upper limit of linearity was about 5 g/L. Adaptation of the Trinder method for glucose to the SMAC is simple and provides an analytically acceptable and economical alternative to the methods ordinarily used with the SMAC.
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PMID:Evaluation of the BMC glucose oxidase/peroxidase-4-aminophenazone-phenol procedure for glucose as adapted to the Technicon SMAC. 47 40

In the determination of unbound bilirubin by rate of oxidation with peroxidase, errors may be caused by (1) phenol, propylparaben, and phenothiazines (free radical acceleration), (2) haemoglobin (peroxidase effect), and (3) ascorbate (inhibition). Such errors may be diminished by dilution 1:40, or with an anti-oxidant, tert-butyl-p-hydroxyanisole, and ascorbate oxidase.
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PMID:Kinetics of bilirubin oxidation with peroxidase, as applied to studies of bilirubin-albumin binding. 52 62


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