Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acetaminophen, p-aminophenol, and oxyphenbutazone interfere with the glucose oxidase/peroxidase method for glucose. Structurally related compounds that lack a free phenolic hydroxyl group (acetanilide, aniline, and phenylbutazone) do not interfere. During the analytical procedure acetaminophen is consumed. One mole of acetaminophen leads to an apparent loss of four moles of glucose. The hexokinase/glucose-6-phosphate dehydrogenase method (Boehringer Hexokinase method) is not affected by these substances.
 ...
PMID:Interference by acetaminophen in the glucose oxidase-peroxidase method for blood glucose determination. 97 21

An amperometric glucose biosensor was fabricated by the electrochemical polymerization of pyrrole onto a platinum electrode in the presence of the enzyme glucose oxidase in a KCl solution at a potential of +0.65 V versus SCE. The enzyme was entrapped into the polypyrrole film during the electropolymerization process. Glucose responses were measured by potentiostating the enzyme electrode at a potential of +0.7 V versus SCE in order to oxidize the hydrogen generated by the oxidation of glucose by the enzyme in the presence of oxygen. Experiments were performed to determine the optimal conditions of the polypyrrole glucose oxidase film preparation (pyrrole and glucose oxidase concentrations in the plating solution) and the response to glucose from such electrodes was evaluated as a function of film thickness, pH and temperature. It was found that a concentration of 0.3 M pyrrole in the presence of 65 U/ml of glucose oxidase in 0.01 M KCl were the optimal parameters for the fabrication of the biosensor. The optimal response was obtained for a film thickness of 0.17 microns (75 mC/cm2) at pH 6 and at a temperature of 313 K. The temperature dependence of the amperometric response indicated an activation energy of 41 kJ/mole. The linearity of the enzyme electrode response ranged from 1.0 mM to 7.5 mM glucose and kinetic parameters determined for the optimized biosensors were 33.4 mM for the Km and 7.2 microA for the Imax. It was demonstrated that the internal diffusion of hydrogen peroxide through the polypyrrole layer to the platinum surface was the main limiting factor controlling the magnitude of the response of the biosensor to glucose. The response was directly related to the enzyme loading in the polypyrrole film. The shelf life and the operational stability of the optimized biosensor exceed 500 days and 175 assays, respectively. The substrate specificity of the entrapped glucose oxidase was not altered by the immobilization procedure.
 ...
PMID:Optimization of a polypyrrole glucose oxidase biosensor. 227 Nov 47

The substitution of glucose-antiglucose oxidase complex (GAG) for peroxidase antiperoxidase (PAP) in the Sternberger three-layer unlabeled antibody method avoids the problems associated with the use of the chromogen 3,3,diaminobenzidine (DAB). The blue final reaction product obtained using the GAG complex is not obscured by melanin granules, which is often the case when using the PAP-DAB combination. The replacement of PAP with GAG complexes facilitates the detection of melanocytes in melanoma and blue nevi. The absence of endogenous glucose oxidase in mammals provides for greater image contrast, which is not possible using alternative chromogens and immunoperoxidase.
 ...
PMID:The substitution of glucose-antiglucose oxidase complex (GAG) for peroxidase-antiperoxidase (PAP) in immunohistochemical studies of skin. 330 93

The hemoglobin Porto Alegre (HbPA) disulfide polymer dodecamer and the HbPA, HbA disulfide polymer octamer subunit dissociation by NaCl was studied by measuring the osmotic pressure of CO-hemoglobin solutions at pH = 6.9 and 20 degrees C. The dissociation equilibrium constants were evaluated from the osmotic pressure data. The subunit dissociation of the two types of disulfide polymers follows a reaction of the type A3 in equilibrium 3A. The HbPA disulfide polymer dodecamer appears to be more susceptible to NaCl induced dissociation than is normal HbA and less resistant to dissociation on protein dilution. The HbPA, HbA disulfide polymer octamer appears to be much more susceptible to dissociation on protein dilution than is the HbPA disulfide polymer dodecamer and normal HbA. The standard free energy of dissociation of the HbPA disulfide polymer at 2 M NaCl is delta GOD(25 degrees C) = 12 kcal/mole. The type of dissociation reaction (A3 in equilibrium with 3A) support the conclusion that the HbPA disulfide polymer has a quaternary molecular structure of a closed ring of three tetramers.
 ...
PMID:Osmometric study of the subunit dissociation of hemoglobin Porto Alegre [beta 9(A6)Ser----Cys] dissulfide polymer. 345 22

The yeast Saccharomyces cerevisiae, produces a cytochrome P-450 enzyme with a Soret peak in the reduced-CO difference spectrum at 448 nm. The enzyme purified to homogeneity (88-97% pure on a specific content basis) has a molecular wt. of 55 500 as determined by SDS-PAGE. Amino acid analysis of yeast cytochrome P-448 revealed 407 amino acid residues per molecule with a 43% complement of hydrophobic residues. Although the number of residues is smaller than cytochrome P-448 enzymes from mammalian sources, the percentage of hydrophobic residues is almost identical. Estimation of the haem content of yeast cytochrome P-448 showed that one haem group was present per molecule. Phospholipid was present at very low levels. The molecular wt. of the polypeptide chain plus an estimated 5-6 units of hexose and of hexosamine is in good agreement with the molecular wt. value obtained from SDS-PAGE. A reconstituted system of purified cytochrome P-448, purified NADPH-cytochrome P-450 (c) reductase and phospholipid showed aryl hydrocarbon hydroxylase activity towards benzo[a]pyrene. Both protein components, NADPH and dilauroyl phosphatidylcholine (or emulgen 911) were necessary for full activity. The NADPH requirement could be replaced by cumene hydroperoxide or H2O2 generated in situ from a glucose oxidase system; in each case Vmax is increased, but the apparent affinity for benzo[a]pyrene, as measured by an increased Km, is lowered. The spin state of purified yeast cytochrome P-448 was 94% low spin (22 degrees C) as determined from the temperature-dependent spin-state equilibrium. The addition of benzo[a]pyrene to this enzyme resulted in a change to higher spin state (18% high spin at 22 degrees C). Equilibrium gel filtration analysis of the number of benzo[a]pyrene binding sites per mole of enzyme monomer showed a value of 1 for purified yeast cytochrome P-448 and 6 for this enzyme in microsomal form. The corresponding values for purified and microsomal cytochrome P-450 from phenobarbital-pretreated rats are 1 and 6, respectively. However, purified cytochrome P-448 from beta-naphthoflavone-induced rats gave a value of 6 benzo[a]pyrene binding sites. Type I binding spectra with purified yeast cytochrome P-448 were observed with benzo[a]pyrene, lanosterol, ethylmorphine, dimethylnitrosamine, sodium phenobarbitone and perhydrofluorene. Type II spectral changes were observed with imidazole, aniline and benzphetamine. Cytochrome P-448 from Saccharomyces cerevisiae is identified as a distinct enzyme of the P-450 family. This enzyme however has many properties in common with cytochrome P-448 from mammalian sources.(ABSTRACT TRUNCATED AT 400 WORDS)
 ...
PMID:Studies on the properties of highly purified cytochrome P-448 and its dependent activity benzo[a]pyrene hydroxylase, from Saccharomyces cerevisiae. 632 93

In addition to the phosphate residues contained in the acid-dissociable FAD and the molybdenum cofactor moieties, milk xanthine oxidase contains one mole of covalently bound phosphorus per active-center molybdenum. Acid hydrolysis of the apoprotein moiety and subsequent analysis by high-voltage thin-layer electrophoresis has identified the phosphorylated amino acid residue to be phosphoserine. 31P NMR data show the phosphopeptide to be monosubstituted, in agreement with the chemical analysis. A pH-dependent chemical shift of the phosphorus residue in the molybdenum cofactor moiety is also observed which provides unequivocal support for suggestions in the literature that this cofactor contains a monosubstituted phosphate. 31P NMR studies on the intact enzyme show phosphorus resonances at about -3 ppm, +1 ppm, +8.8 ppm and at +13.5 ppm. The resonances at +8.8 ppm and at +13.5 ppm are assigned to those of the pyrophosphate linkage of the FAD moiety by analogy with chemical shift data of the FAD on glucose oxidase [James, T.L., Edmondson, D.E., and Husain, M. (1981) Biochemistry 20, 617] and from the absence of any resonances in this region upon examination of preparations of deflavo xanthine oxidase. The intensity and resolution of the resonance at about -3 ppm is dependent on the degree of functionality of the enzyme. This resonance has a small amplitude relative to the FAD resonances in 50-60% functional enzyme, but increases dramatically in intensity in the desulpho enzyme. This resonance is the only one exposed to solvent as it is the only one susceptible to paramagnetic line-broadening on the addition of Mn(II) to the enzyme solution. Treatment of the enzyme with allopurinol leads to alteration of the approximately equal to -3-ppm resonance, but does not significantly affect the other resonances. Formation of the stable Mo(V) 'inhibited' form of the enzyme with ethylene glycol results in extensive line-broadening of the resonances at -3 ppm and +1 ppm, but has no observable affect on the FAD resonances. These data suggest that in addition to the phosphate on the molybdenum cofactor, the phosphoserine residue in xanthine oxidase is also in close proximity to the activesite molybdenum center of this enzyme. These results are discussed with respect to possible implications on the catalytic mechanism of the enzyme.
 ...
PMID:31P nuclear magnetic resonance and chemical studies of the phosphorus residues in bovine milk xanthine oxidase. 654 6

An enzyme glucose microsensor using a glucose oxidase-immobilized porous carbon/Teflon composite microelectrode was developed. The microsensor was fabricated by etching a platinum microelectrode (platinum, radius of 25 and 50 micrometers) in hot aqua regia to create a cavity at the tip and then packing a porous carbon/Teflon composite, which was made from acetylene black and Teflon emulsion, into the cavity. Nafion was impregnated into the inner surface of porous carbon/Teflon composite electrode following immobilization of Os(bpy)3+2/+3 as electron transfer mediators. The loading amount of Os(bpy)3+2/+3 in the Nafion/porous carbon/Teflon composite electrode was found to be 7.0x10(-8) mole cm(-2), which is much higher than that in polymer modified electrodes reported in literatures. The microsensor was further dipped overnight in buffer solution containing glucose oxidase for enzyme modification. With both glucose oxidase and mediators in the porous carbon/Teflon composite surface, the sensor performance was evaluated in buffer solutions containing different glucose concentrations and serum samples for glucose determination. The microsensor showed directly electrochemical glucose oxidation on the Os(bpy)3+2/+3 impregnated enzyme/porous carbon/Teflon composite surface with linear response over concentration range of 0-15 mM and Machaelis behavior. Reliability and reproducibility were conducted in serum samples and glucose buffer solution, and the results demonstrated there was no significant decrease of amperometric response in air-saturated solution for one month. The sensor demonstrated potential in clinical diagnostic applications.
 ...
PMID:Porous carbon composite/enzyme glucose microsensor. 1535 60

An enzyme glucose microsensor using a glucose oxidase-immobilized porous carbon/Teflon composite microelectrode was developed. The microsensor was fabricated by etching a platinum microelectrode (platinum, radius of 25 and 50 micrometers) in hot aqua regia to create a cavity at the tip and then packing a porous carbon/Teflon composite, which was made from acetylene black and Teflon emulsion, into the cavity. Nafion was impregnated into the inner surface of porous carbon/Teflon composite electrode following immobilization of Os(bpy)3+2/+3 as electron transfer mediators. The loading amount of Os(bpy)3+2/+3 in the Nafion/porous carbon/Teflon composite electrode was found to be 7.0x10(-8) mole cm(-2), which is much higher than that in polymer modified electrodes reported in literatures. The microsensor was further dipped overnight in buffer solution containing glucose oxidase for enzyme modification. With both glucose oxidase and mediators in the porous carbon/Teflon composite surface, the sensor performance was evaluated in buffer solutions containing different glucose concentrations and serum samples for glucose determination. The microsensor showed directly electrochemical glucose oxidation on the Os(bpy)3+2/+3 impregnated enzyme/porous carbon/Teflon composite surface with linear response over concentration range of 0-15 mM and Machaelis behavior. Reliability and reproducibility were conducted in serum samples and glucose buffer solution, and the results demonstrated there was no significant decrease of amperometric response in air-saturated solution for one month. The sensor demonstrated potential in clinical diagnostic applications.
 ...
PMID:Porous carbon composite/enzyme glucose microsensor. 1535 71

The time course of the peroxidative bromination of propylene accompanied by in situ generation of hydrogen peroxide by glucose oxidase was examined to improve the productivity of propylene bromohydrin. To prevent the rapid inactivation of lactoperoxidase by excess hydrogen peroxide, it was effective to use lactoperoxidase in large excess as compared with glucose oxidase, and to raise the concentration of bromide ion. However, the rate of glucose consumption was lowered at high concentrations of bromide ion, and at higher mole fraction of oxygen as compared with propylene in the gas mixture. Therefore, it seemed that for the favorable production of bromohydrin there existed the optimal conditions for the concentration of bromide ion and for the composition of oxygen-propylene gas mixture. Such kinetic behaviors of the sequential enzymatic reactions were explained by a mechanism involving free hypobromous acid as a reactive intermediate. Furthermore, the stability of the coimmobilized enzymes with k-carrageenan gels was investigated in continuous operations. The half-life of the enzymes was ca. 60 h for the production of propylene bromohydrin.
 ...
PMID:Enzymatic formation of propylene bromohydrin from propylene by glucose oxidase and lactoperoxidase. 1855 22

Glucose oxidase (E.C. 1.1.3.4) is reversibly immobilized in a reactor coupled to a flow-injection analysis system using an immunological reaction. The antibody used is irreversibly immobilized on the reactor support by an avidin-biotin linkage. The bond between avidin and biotin is nearly irreversible under normal elution conditions for antibody-antigen reactions. The reactor is packed with a support on which avidin is covalently attached and a biotin-bound second antibody is passed over the reactor packing, which immobilizes this antibody. An immune complex of the enzyme, or first anti-enzyme antibody followed separately by enzyme, is introduced into the flow system, resulting in enzyme immobilization. The reactor produced can be used in the determination of 1 x 10(-11) -1 x 10(-6) mole of glucose with a sample size of 20 mul and a sample throughput of 20-30/hr. These results are comparable to or better than those obtained with glucose oxidase directly immobilized on the same support. The enzyme can be removed by elution with low-pH buffers, and the reactor regenerated by injection of the anti-enzyme antibody and the enzyme.
 ...
PMID:Strategies for the reversible immobilization of enzymes by use of biotin-bound anti-enzyme antibodies. 1896 97


1 2 Next >>