An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC
Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.
An imperfect fungus causing smut or black mold of several fruits, vegetables, etc.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.
Glucose in blood.
Any of a variety of procedures which use biomolecular probes to measure the presence or concentration of biological molecules, biological structures, microorganisms, etc., by translating a biochemical interaction at the probe surface into a quantifiable physical signal.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria.
An enzyme derived from cow's milk. It catalyzes the radioiodination of tyrosine and its derivatives and of peptides containing tyrosine.
Electric conductors through which electric currents enter or leave a medium, whether it be an electrolytic solution, solid, molten mass, gas, or vacuum.
Method of analyzing chemicals using automation.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC; EC; EC and EC
A test to determine the ability of an individual to maintain HOMEOSTASIS of BLOOD GLUCOSE. It includes measuring blood glucose levels in a fasting state, and at prescribed intervals before and after oral glucose intake (75 or 100 g) or intravenous infusion (0.5 g/kg).
A mitosporic Trichocomaceae fungal genus that develops fruiting organs resembling a broom. When identified, teleomorphs include EUPENICILLIUM and TALAROMYCES. Several species (but especially PENICILLIUM CHRYSOGENUM) are sources of the antibiotic penicillin.
D-Amino-Acid Oxidase is an enzyme that catalyzes the oxidative deamination of D-amino acids to their corresponding α-keto acids, ammonia, and hydrogen peroxide, playing a crucial role in the metabolism of non-proteinogenic D-amino acids.
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC
The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.
An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide. EC
An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A pathological state in which BLOOD GLUCOSE level is less than approximately 140 mg/100 ml of PLASMA at fasting, and above approximately 200 mg/100 ml plasma at 30-, 60-, or 90-minute during a GLUCOSE TOLERANCE TEST. This condition is seen frequently in DIABETES MELLITUS, but also occurs with other diseases and MALNUTRITION.
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide to water, while oxidizing various organic and inorganic compounds, playing crucial roles in diverse biological processes including stress response, immune defense, and biosynthetic reactions.
An aldehyde oxidoreductase expressed predominantly in the LIVER; LUNGS; and KIDNEY. It catalyzes the oxidation of a variety of organic aldehydes and N-heterocyclic compounds to CARBOXYLIC ACIDS, and also oxidizes quinoline and pyridine derivatives. The enzyme utilizes molybdenum cofactor and FAD as cofactors.
An electrochemical technique for measuring the current that flows in solution as a function of an applied voltage. The observed polarographic wave, resulting from the electrochemical response, depends on the way voltage is applied (linear sweep or differential pulse) and the type of electrode used. Usually a mercury drop electrode is used.
The rate dynamics in chemical or physical systems.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Narrow pieces of material impregnated or covered with a substance used to produce a chemical reaction. The strips are used in detecting, measuring, producing, etc., other substances. (From Dorland, 28th ed)
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
The appearance of an abnormally large amount of GLUCOSE in the urine, such as more than 500 mg/day in adults. It can be due to HYPERGLYCEMIA or genetic defects in renal reabsorption (RENAL GLYCOSURIA).
An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.
Inorganic salts of the hypothetical acid ferrocyanic acid (H4Fe(CN)6).
Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499)
An enzyme that catalyzes the conversion of ATP and a D-hexose to ADP and a D-hexose 6-phosphate. D-Glucose, D-mannose, D-fructose, sorbitol, and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase. (From Enzyme Nomenclature, 1992) EC
Flavoproteins are a type of protein molecule that contain noncovalently bound flavin mononucleotide or flavin adenine dinucleotide as cofactors, involved in various redox reactions and metabolic pathways, such as electron transfer, energy production, and DNA repair.
A ubiquitously expressed glucose transporter that is important for constitutive, basal GLUCOSE transport. It is predominately expressed in ENDOTHELIAL CELLS and ERYTHROCYTES at the BLOOD-BRAIN BARRIER and is responsible for GLUCOSE entry into the BRAIN.
Platinum. A heavy, soft, whitish metal, resembling tin, atomic number 78, atomic weight 195.09, symbol Pt. (From Dorland, 28th ed) It is used in manufacturing equipment for laboratory and industrial use. It occurs as a black powder (platinum black) and as a spongy substance (spongy platinum) and may have been known in Pliny's time as "alutiae".
A generic term for a variety of compounds that contain silicon, oxygen, and magnesium, and may contain hydrogen. Examples include TALC and some kinds of ASBESTOS.

Expression of two major chitinase genes of Trichoderma atroviride (T. harzianum P1) is triggered by different regulatory signals. (1/420)

Regulation of the expression of the two major chitinase genes, ech42 (encoding the CHIT42 endochitinase) and nag1 (encoding the CHIT73 N-acetyl-beta-D-glucosaminidase), of the chitinolytic system of the mycoparasitic biocontrol fungus Trichoderma atroviride (= Trichoderma harzianum P1) was investigated by using a reporter system based on the Aspergillus niger glucose oxidase. Strains harboring fusions of the ech42 or nag1 5' upstream noncoding sequences with the A. niger goxA gene displayed a glucose oxidase activity pattern that was consistent under various conditions with expression of the native ech42 and nag1 genes, as assayed by Northern analysis. The expression product of goxA in the mutants was completely secreted into the medium, detectable on Western blots, and quantifiable by enzyme-linked immunosorbent assay. nag1 gene expression was triggered during growth on fungal (Botrytis cinerea) cell walls and on the chitin degradation product N-acetylglucosamine. N-Acetylglucosamine, di-N-acetylchitobiose, or tri-N-acetylchitotriose also induced nag1 gene expression when added to mycelia pregrown on different carbon sources. ech42 expression was also observed during growth on fungal cell walls but, in contrast, was not triggered by addition of chitooligomers to pregrown mycelia. Significant ech42 expression was observed after prolonged carbon starvation, independent of the use of glucose or glycerol as a carbon source, suggesting that relief of carbon catabolite repression was not involved in induction during starvation. In addition, ech42 gene transcription was triggered by physiological stress, such as low temperature, high osmotic pressure, or the addition of ethanol. Four copies of a putative stress response element (CCCCT) were found in the ech42 promoter.  (+info)

Strictures in Crohn's disease are characterised by an accumulation of mast cells colocalised with laminin but not with fibronectin or vitronectin. (2/420)

BACKGROUND/AIMS: Intestinal fibrosis and stricture formation is an unresolved problem in Crohn's disease. The aim of this study was to investigate whether mast cells accumulate in these tissues and whether their localisation is associated with extracellular matrix components. METHODS: Mast cells were visualised by immunohistochemical staining of the mast cell specific proteases chymase and tryptase. Their localisation in relation to extracellular matrix components was shown by immunohistochemical double labelling. RESULTS: In strictures in Crohn's disease, a striking accumulation of mast cells was seen particularly in the hypertrophied and fibrotic muscularis propria, with a mean (SEM) mast cell number of 81.3 (14.9) v 1.5 (0.9)/mm(2) in normal bowel (p<0.0005). All mast cells in the muscularis propria were colocalised with patches of laminin. In contrast, in the submucosa, laminin was exclusively found in the basal lamina of blood vessels where many adherent mast cells were seen. No colocalisation of mast cells was found with fibronectin or vitronectin. CONCLUSIONS: The large accumulation of mast cells in the muscle layer of strictured bowel suggests a functional role for these cells in the hypertrophic and fibrotic response of the smooth muscle cells. The colocalisation with laminin indicates a mechanism of interaction between smooth muscle cells and mast cells that may be important in the role of mast cells in the process of fibrosis.  (+info)

Hydrogen peroxide production from reactive liposomes encapsulating enzymes. (3/420)

Reactive cationic and anionic liposomes have been prepared from mixtures of dimyristoylphosphatidylcholine (DMPC) and cholesterol incorporating dimethyldioctadecylammonium bromide and DMPC incorporating phosphatidylinositol, respectively. The liposomes were prepared by the vesicle extrusion technique and had the enzymes glucose oxidase (GO) encapsulated in combination with horseradish peroxidase (HRP) or lactoperoxidase (LPO). The generation of hydrogen peroxide from the liposomes in response to externally added D-glucose substrate was monitored using a Rank electrode system polarised to +650 mV, relative to a standard silver-silver chloride electrode. The effects of encapsulated enzyme concentration, enzyme combinations (GO+HRP, GO+LPO), substrate concentration, electron donor and temperature on the production of hydrogen peroxide have been investigated. The electrode signal (peroxide production) was found to increase linearly with GO incorporation, was reduced on addition of HRP and an electron donor (o-dianisidine) and showed a maximum at the lipid chain-melting temperature from the anionic liposomes containing no cholesterol. To aid interpretation of the results, the permeability of the non-reactive substrate (methyl glucoside) across the bilayer membranes was measured. It was found that the encapsulation of the enzymes effected the permeability coefficients of methyl glucoside, increasing them in the case of anionic liposomes and decreasing them in the case of cationic liposomes. These observations are discussed in terms of enzyme bilayer interactions.  (+info)

Immunotargeting of glucose oxidase: intracellular production of H(2)O(2) and endothelial oxidative stress. (4/420)

Extracellular and intracellular reactive oxygen species attack different targets and may, therefore, result in different forms of oxidative stress. To specifically study an oxidative stress induced by a regulated intracellular flux of a defined reactive oxygen species in endothelium, we used immunotargeting of the H(2)O(2)-generating enzyme glucose oxidase (GOX) conjugated with an antibody to platelet-endothelial cell adhesion molecule (PECAM)-1, an endothelial surface antigen. Anti-PECAM-(125)I-GOX conjugates specifically bind to both endothelial and PECAM-transfected cells. Approximately 70% of cell-bound anti-PECAM-(125)I-GOX was internalized. The cell-bound conjugate was enzymatically active and generated H(2)O(2) from glucose. Use of the fluorescent dye dihydrorhodamine 123 revealed that 70% of H(2)O(2) was generated intracellularly, whereas 30% of H(2)O(2) was detected in the cell medium. Catalase added to the cells eliminated H(2)O(2) in the medium but had little effect on the intracellular generation of H(2)O(2) by anti-PECAM-GOX. Both H(2)O(2) added exogenously to the cell medium (extracellular H(2)O(2)) and that generated by anti-PECAM-GOX caused oxidative stress manifested by time- and dose-dependent irreversible plasma membrane damage. Inactivation of cellular catalase by aminotriazole treatment augmented damage caused by either extracellular H(2)O(2) or anti-PECAM-GOX. Catalase added to the medium protected either normal or aminotriazole-treated cells against extracellular H(2)O(2), yet failed to protect cells against injury induced by anti-PECAM-GOX. Therefore, treatment of PECAM-positive cells with anti-PECAM-GOX leads to conjugate internalization, predominantly intracellular H(2)O(2) generation and intracellular oxidative stress. These results indicate that anti-PECAM-GOX 1) provides cell-specific intracellular delivery of an active enzyme and 2) causes intracellular oxidative stress in PECAM-positive cells.  (+info)

Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honeybee (Apis mellifera L.). (5/420)

Worker honeybees change their behaviour from the role of nurse to that of forager with age. We have isolated cDNA clones for two honeybee (Apis mellifera L.) genes, encoding alpha-amylase and glucose oxidase homologues, that are expressed in the hypopharyngeal gland of forager bees. The predicted amino acid sequence of the putative Apis amylase showed 60.5% identity with Drosophila melanogaster alpha-amylase, whereas that of Apis glucose oxidase showed 23.8% identity with Aspergillus niger glucose oxidase. To determine whether the isolated cDNAs actually encode these enzymes, we purified amylase and glucose oxidase from homogenized forager-bee hypopharyngeal glands. We sequenced the N-terminal regions of the purified enzymes and found that they matched the corresponding cDNAs. mRNAs for both enzymes were detected by Northern blotting in the hypopharyngeal gland of the forager bee but not in the nurse-bee gland. These results clearly indicate that expression of the genes for these carbohydrate-metabolizing enzymes, which are needed to process nectar into honey, in the hypopharyngeal gland is associated with the age-dependent role change of the worker.  (+info)

Second harmonic generation of glucose oxidase at the air/water interface. (6/420)

We present a study of the adsorption of the glucose oxidase enzyme (GOx) at the air/water interface, using the nonlinear optical technique of surface second harmonic generation (SSHG). Resonant SSHG experiments were achieved by probing the pi-pi* transition of the flavin adenine dinucleotide (FAD) chromophores embedded in the GOx protein. Because of the subsequent resonance enhancement of the signal, the second harmonic (SH) wave arising from the GOx entities adsorbed at the interface was detectable for protein bulk aqueous concentrations as low as 70 nM. The protein adsorption was followed, and, at high GOx coverage, a change in the orientation of the FAD chromophore was observed, indicating either a rearrangement or a reorientation of the protein at the interface. Inasmuch as GOx is negatively charged at the biological pH of 7, its interactions with charged surfactants were also investigated. As expected, spreading positively charged surfactants onto a partial protein monolayer was found to increase the GOx surface concentration, whereas in the case of negatively charged surfactants, the GOx surface concentration decreased until the SH signal went back to the pure buffer solution response level. With the increasing GOx surface concentration, the rearrangement or reorientation of the protein was also observed.  (+info)

Imaging of biological macromolecules on mica in humid air by scanning electrochemical microscopy. (7/420)

Imaging of DNA, keyhole limpet hemocyanin, mouse monoclonal IgG, and glucose oxidase on a mica substrate has been accomplished by scanning electrochemical microscopy with a tungsten tip. The technique requires the use of a high relative humidity to form a thin film of water on the mica surface that allows electrochemical reactions to take place at the tip and produce a faradaic current (approximately 1 pA) that can be used to control tip position. The effect of relative humidity and surface pretreatment with buffer solutions on the ionic conductivity of a mica surface was investigated to find appropriate conditions for imaging. Resolution of the order of 1 nm was obtained.  (+info)

Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose. (8/420)

The effects of mutation of key conserved active-site residues (Tyr-73, Phe-418, Trp-430, Arg-516, Asn-518, His-520 and His-563) of glucose oxidase from Penicillium amagasakiense on substrate binding were investigated. Kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling showed the side chain of Arg-516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be absolutely essential for the efficient binding of beta-D-glucose. The R516K variant, whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80-fold higher apparent K(m) (513 mM) but a V(max) only 70% lower (280 units/mg) than the wild type. The complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effected a 120-fold increase in the apparent K(m) for glucose (to 733 mM) and a decrease in the V(max) to 1/30 (33 units/mg). None of the other substitutions, with the exception of variant F418A, affected the apparent K(m) more than 6-fold. In contrast, the removal of aromatic or bulky residues at positions 73, 418 or 430 resulted in decreases in the maximum rates of glucose oxidation to less than 1/90. Variants of the potentially catalytically active His-520 and His-563 were completely, or almost completely, inactive. Thus, of the residues forming the active site of glucose oxidase, Arg-516 is the most critical amino acid for the efficient binding of beta-D-glucose by the enzyme, whereas aromatic residues at positions 73, 418 and 430 are important for the correct orientation and maximal velocity of glucose oxidation.  (+info)

Glucose oxidase (GOD) is an enzyme that catalyzes the oxidation of D-glucose to D-glucono-1,5-lactone, while reducing oxygen to hydrogen peroxide in the process. This reaction is a part of the metabolic pathway in some organisms that convert glucose into energy. The systematic name for this enzyme is D-glucose:oxygen 1-oxidoreductase.

Glucose oxidase is commonly found in certain fungi, such as Aspergillus niger, and it has various applications in industry, medicine, and research. For instance, it's used in the production of glucose sensors for monitoring blood sugar levels, in the detection and quantification of glucose in food and beverages, and in the development of biosensors for environmental monitoring.

It's worth noting that while glucose oxidase has many applications, it should not be confused with glutathione peroxidase, another enzyme involved in the reduction of hydrogen peroxide to water.

Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.

Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.

Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.

Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.

'Aspergillus niger' is a species of fungi that belongs to the genus Aspergillus. It is a ubiquitous microorganism that can be found in various environments, including soil, decaying vegetation, and indoor air. 'Aspergillus niger' is a black-colored mold that produces spores that are easily dispersed in the air.

This fungus is well known for its ability to produce a variety of enzymes and metabolites, some of which have industrial applications. For example, it is used in the production of citric acid, which is widely used as a food additive and preservative.

However, 'Aspergillus niger' can also cause health problems in humans, particularly in individuals with weakened immune systems or underlying lung conditions. It can cause allergic reactions, respiratory symptoms, and invasive aspergillosis, a serious infection that can spread to other organs in the body.

In addition, 'Aspergillus niger' can produce mycotoxins, which are toxic compounds that can contaminate food and feed and cause various health effects in humans and animals. Therefore, it is important to prevent the growth and proliferation of this fungus in indoor environments and food production facilities.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

NADPH oxidase is an enzyme complex that plays a crucial role in the production of reactive oxygen species (ROS) in various cell types. The primary function of NADPH oxidase is to catalyze the transfer of electrons from NADPH to molecular oxygen, resulting in the formation of superoxide radicals. This enzyme complex consists of several subunits, including two membrane-bound components (gp91phox and p22phox) and several cytosolic components (p47phox, p67phox, p40phox, and rac1 or rac2). Upon activation, these subunits assemble to form a functional enzyme complex that generates ROS, which serve as important signaling molecules in various cellular processes. However, excessive or uncontrolled production of ROS by NADPH oxidase has been implicated in the pathogenesis of several diseases, such as cardiovascular disorders, neurodegenerative diseases, and cancer.

Blood glucose, also known as blood sugar, is the concentration of glucose in the blood. Glucose is a simple sugar that serves as the main source of energy for the body's cells. It is carried to each cell through the bloodstream and is absorbed into the cells with the help of insulin, a hormone produced by the pancreas.

The normal range for blood glucose levels in humans is typically between 70 and 130 milligrams per deciliter (mg/dL) when fasting, and less than 180 mg/dL after meals. Levels that are consistently higher than this may indicate diabetes or other metabolic disorders.

Blood glucose levels can be measured through a variety of methods, including fingerstick blood tests, continuous glucose monitoring systems, and laboratory tests. Regular monitoring of blood glucose levels is important for people with diabetes to help manage their condition and prevent complications.

Biosensing techniques refer to the methods and technologies used to detect and measure biological molecules or processes, typically through the use of a physical device or sensor. These techniques often involve the conversion of a biological response into an electrical signal that can be measured and analyzed. Examples of biosensing techniques include electrochemical biosensors, optical biosensors, and piezoelectric biosensors.

Electrochemical biosensors measure the electrical current or potential generated by a biochemical reaction at an electrode surface. This type of biosensor typically consists of a biological recognition element, such as an enzyme or antibody, that is immobilized on the electrode surface and interacts with the target analyte to produce an electrical signal.

Optical biosensors measure changes in light intensity or wavelength that occur when a biochemical reaction takes place. This type of biosensor can be based on various optical principles, such as absorbance, fluorescence, or surface plasmon resonance (SPR).

Piezoelectric biosensors measure changes in mass or frequency that occur when a biomolecule binds to the surface of a piezoelectric crystal. This type of biosensor is based on the principle that piezoelectric materials generate an electrical charge when subjected to mechanical stress, and this charge can be used to detect changes in mass or frequency that are proportional to the amount of biomolecule bound to the surface.

Biosensing techniques have a wide range of applications in fields such as medicine, environmental monitoring, food safety, and biodefense. They can be used to detect and measure a variety of biological molecules, including proteins, nucleic acids, hormones, and small molecules, as well as to monitor biological processes such as cell growth or metabolism.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

Hydrogen peroxide (H2O2) is a colorless, odorless, clear liquid with a slightly sweet taste, although drinking it is harmful and can cause poisoning. It is a weak oxidizing agent and is used as an antiseptic and a bleaching agent. In diluted form, it is used to disinfect wounds and kill bacteria and viruses on the skin; in higher concentrations, it can be used to bleach hair or remove stains from clothing. It is also used as a propellant in rocketry and in certain industrial processes. Chemically, hydrogen peroxide is composed of two hydrogen atoms and two oxygen atoms, and it is structurally similar to water (H2O), with an extra oxygen atom. This gives it its oxidizing properties, as the additional oxygen can be released and used to react with other substances.

Xanthine oxidase is an enzyme that catalyzes the oxidation of xanthine to uric acid, which is the last step in purine metabolism. It's a type of molybdenum-containing oxidoreductase that generates reactive oxygen species (ROS) during its reaction mechanism.

The enzyme exists in two interconvertible forms: an oxidized state and a reduced state. The oxidized form, called xanthine oxidase, reduces molecular oxygen to superoxide and hydrogen peroxide, while the reduced form, called xanthine dehydrogenase, reduces NAD+ to NADH.

Xanthine oxidase is found in various tissues, including the liver, intestines, and milk. An overproduction of uric acid due to increased activity of xanthine oxidase can lead to hyperuricemia, which may result in gout or kidney stones. Some medications and natural compounds are known to inhibit xanthine oxidase, such as allopurinol and febuxostat, which are used to treat gout and prevent the formation of uric acid stones in the kidneys.

Lactoperoxidase is a type of peroxidase enzyme that is present in various secretory fluids, including milk, saliva, and tears. In milk, lactoperoxidase plays an important role in the natural defense system by helping to protect against microbial growth. It does this by catalyzing the oxidation of thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which is a potent antimicrobial agent.

Lactoperoxidase is a glycoprotein with a molecular weight of approximately 78 kDa, and it is composed of four identical subunits, each containing a heme group that binds to the hydrogen peroxide molecule during the enzymatic reaction. Lactoperoxidase has been studied for its potential therapeutic applications in various fields, including oral health, food preservation, and wound healing.

An electrode is a medical device that can conduct electrical currents and is used to transmit or receive electrical signals, often in the context of medical procedures or treatments. In a medical setting, electrodes may be used for a variety of purposes, such as:

1. Recording electrical activity in the body: Electrodes can be attached to the skin or inserted into body tissues to measure electrical signals produced by the heart, brain, muscles, or nerves. This information can be used to diagnose medical conditions, monitor the effectiveness of treatments, or guide medical procedures.
2. Stimulating nerve or muscle activity: Electrodes can be used to deliver electrical impulses to nerves or muscles, which can help to restore function or alleviate symptoms in people with certain medical conditions. For example, electrodes may be used to stimulate the nerves that control bladder function in people with spinal cord injuries, or to stimulate muscles in people with muscle weakness or paralysis.
3. Administering treatments: Electrodes can also be used to deliver therapeutic treatments, such as transcranial magnetic stimulation (TMS) for depression or deep brain stimulation (DBS) for movement disorders like Parkinson's disease. In these procedures, electrodes are implanted in specific areas of the brain and connected to a device that generates electrical impulses, which can help to regulate abnormal brain activity and improve symptoms.

Overall, electrodes play an important role in many medical procedures and treatments, allowing healthcare professionals to diagnose and treat a wide range of conditions that affect the body's electrical systems.

"Autoanalysis" is not a term that is widely used in the medical field. However, in psychology and psychotherapy, "autoanalysis" refers to the process of self-analysis or self-examination, where an individual analyzes their own thoughts, feelings, behaviors, and experiences to gain insight into their unconscious mind and understand their motivations, conflicts, and emotional patterns.

Self-analysis can involve various techniques such as introspection, journaling, meditation, dream analysis, and reflection on past experiences. While autoanalysis can be a useful tool for personal growth and self-awareness, it is generally considered less reliable and comprehensive than professional psychotherapy or psychoanalysis, which involves a trained therapist or analyst who can provide objective feedback, interpretation, and guidance.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

A Glucose Tolerance Test (GTT) is a medical test used to diagnose prediabetes, type 2 diabetes, and gestational diabetes. It measures how well your body is able to process glucose, which is a type of sugar.

During the test, you will be asked to fast (not eat or drink anything except water) for at least eight hours before the test. Then, a healthcare professional will take a blood sample to measure your fasting blood sugar level. After that, you will be given a sugary drink containing a specific amount of glucose. Your blood sugar levels will be measured again after two hours and sometimes also after one hour.

The results of the test will indicate how well your body is able to process the glucose and whether you have normal, impaired, or diabetic glucose tolerance. If your blood sugar levels are higher than normal but not high enough to be diagnosed with diabetes, you may have prediabetes, which means that you are at increased risk of developing type 2 diabetes in the future.

It is important to note that a Glucose Tolerance Test should be performed under the supervision of a healthcare professional, as high blood sugar levels can be dangerous if not properly managed.

"Penicillium" is not a medical term per se, but it is a genus of mold that is widely used in the field of medicine, specifically in the production of antibiotics. Here's a scientific definition:

Penicillium is a genus of ascomycete fungi that are commonly found in the environment, particularly in soil, decaying vegetation, and food. Many species of Penicillium produce penicillin, a group of antibiotics with activity against gram-positive bacteria. The discovery and isolation of penicillin from Penicillium notatum by Alexander Fleming in 1928 revolutionized the field of medicine and led to the development of modern antibiotic therapy. Since then, various species of Penicillium have been used in the industrial production of penicillin and other antibiotics, as well as in the production of enzymes, organic acids, and other industrial products.

D-amino-acid oxidase (DAAO) is an enzyme that catalyzes the oxidative deamination of D-amino acids to their corresponding α-keto acids, ammonia, and hydrogen peroxide. This enzyme plays a crucial role in the metabolism of D-amino acids in various organisms, including humans. In humans, DAAO is primarily expressed in the brain and contributes to the regulation of neurotransmitter levels and other physiological processes. Genetic variations and dysregulation of DAAO have been implicated in several neurological disorders, such as schizophrenia and bipolar disorder.

Monoamine oxidase (MAO) is an enzyme found on the outer membrane of mitochondria in cells throughout the body, but primarily in the gastrointestinal tract, liver, and central nervous system. It plays a crucial role in the metabolism of neurotransmitters and dietary amines by catalyzing the oxidative deamination of monoamines. This enzyme exists in two forms: MAO-A and MAO-B, each with distinct substrate preferences and tissue distributions.

MAO-A preferentially metabolizes serotonin, norepinephrine, and dopamine, while MAO-B is mainly responsible for breaking down phenethylamines and benzylamines, as well as dopamine in some cases. Inhibition of these enzymes can lead to increased neurotransmitter levels in the synaptic cleft, which has implications for various psychiatric and neurological conditions, such as depression and Parkinson's disease. However, MAO inhibitors must be used with caution due to their potential to cause serious adverse effects, including hypertensive crises, when combined with certain foods or medications containing dietary amines or sympathomimetic agents.

Electrochemistry is a branch of chemistry that deals with the interconversion of electrical energy and chemical energy. It involves the study of chemical processes that cause electrons to move, resulting in the transfer of electrical charge, and the reverse processes by which electrical energy can be used to drive chemical reactions. This field encompasses various phenomena such as the generation of electricity from chemical sources (as in batteries), the electrolysis of substances, and corrosion. Electrochemical reactions are fundamental to many technologies, including energy storage and conversion, environmental protection, and medical diagnostics.

Protein-Lysine 6-Oxidase (PLOX) is an enzyme that belongs to the family of copper-containing oxidases. It catalyzes the oxidative deamination of specific lysine residues in proteins, resulting in the formation of lysine-6-aldehydes, ammonia, and hydrogen peroxide. This enzyme plays a crucial role in various biological processes, including the regulation of protein function, modification of extracellular matrices, and the maintenance of copper homeostasis. Mutations in the gene encoding PLOX have been associated with certain diseases, such as Menkes disease, a rare X-linked recessive disorder characterized by copper deficiency and neurological symptoms.

Catalase is a type of enzyme that is found in many living organisms, including humans. Its primary function is to catalyze the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from the harmful effects of hydrogen peroxide, which can be toxic at high concentrations.

The chemical reaction catalyzed by catalase can be represented as follows:

H2O2 + Catalase → H2O + O2 + Catalase

Catalase is a powerful antioxidant enzyme that plays an important role in protecting cells from oxidative damage. It is found in high concentrations in tissues that produce or are exposed to hydrogen peroxide, such as the liver, kidneys, and erythrocytes (red blood cells).

Deficiency in catalase activity has been linked to several diseases, including cancer, neurodegenerative disorders, and aging. On the other hand, overexpression of catalase has been shown to have potential therapeutic benefits in various disease models, such as reducing inflammation and oxidative stress.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Glucose intolerance is a condition in which the body has difficulty processing and using glucose, or blood sugar, effectively. This results in higher than normal levels of glucose in the blood after eating, particularly after meals that are high in carbohydrates. Glucose intolerance can be an early sign of developing diabetes, specifically type 2 diabetes, and it may also indicate other metabolic disorders such as prediabetes or insulin resistance.

In a healthy individual, the pancreas produces insulin to help regulate blood sugar levels by facilitating glucose uptake in muscles, fat tissue, and the liver. When someone has glucose intolerance, their body may not produce enough insulin, or their cells may have become less responsive to insulin (insulin resistance), leading to impaired glucose metabolism.

Glucose intolerance can be diagnosed through various tests, including the oral glucose tolerance test (OGTT) and hemoglobin A1c (HbA1c) test. Treatment for glucose intolerance often involves lifestyle modifications such as weight loss, increased physical activity, and a balanced diet with reduced sugar and refined carbohydrate intake. In some cases, medication may be prescribed to help manage blood sugar levels more effectively.

Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide (H2O2) as the electron acceptor. These enzymes contain a heme prosthetic group, which plays a crucial role in their catalytic activity. Peroxidases are widely distributed in nature and can be found in plants, animals, and microorganisms. They play important roles in various biological processes, including defense against oxidative stress, lignin degradation, and host-pathogen interactions. Some common examples of peroxidases include glutathione peroxidase, which helps protect cells from oxidative damage, and horseradish peroxidase, which is often used in laboratory research.

Aldehyde oxidase is an enzyme found in the liver and other organs that helps to metabolize (break down) various substances, including drugs, alcohol, and environmental toxins. It does this by catalyzing the oxidation of aldehydes, which are organic compounds containing a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bond to an oxygen atom. Aldehyde oxidase is a member of the molybdenum-containing oxidoreductase family, which also includes xanthine oxidase and sulfite oxidase. These enzymes all contain a molybdenum cofactor that plays a critical role in their catalytic activity.

Aldehyde oxidase is an important enzyme in the metabolism of many drugs, as it can convert them into more water-soluble compounds that can be easily excreted from the body. However, variations in the activity of this enzyme between individuals can lead to differences in drug metabolism and response. Some people may have higher or lower levels of aldehyde oxidase activity, which can affect how quickly they metabolize certain drugs and whether they experience adverse effects.

In addition to its role in drug metabolism, aldehyde oxidase has been implicated in the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. For example, elevated levels of aldehydes produced by lipid peroxidation have been linked to oxidative stress and inflammation, which can contribute to the progression of these conditions. Aldehyde oxidase may also play a role in the detoxification of environmental pollutants, such as polycyclic aromatic hydrocarbons (PAHs) and heterocyclic amines (HCAs), which have been associated with an increased risk of cancer.

Overall, aldehyde oxidase is an important enzyme that plays a critical role in the metabolism of drugs and other substances, as well as in the development of various diseases. Understanding its activity and regulation may help to develop new strategies for treating or preventing these conditions.

Polarography is a type of electrochemical analysis technique used to determine the concentration of an ion or electron-transferring species in a solution. It involves measuring the current that flows through an electrode as the voltage is varied, which can provide information about the redox potential and the number of electrons transferred during a reaction. The technique is particularly useful for analyzing complex mixtures and for detecting trace amounts of substances.

In polarography, a dropping mercury electrode (DME) is typically used as the working electrode. As the mercury droplets fall from the electrode, they create fresh surfaces for analysis, which helps to minimize interference from surface-adsorbed species. The DME is immersed in a solution containing the analyte along with a supporting electrolyte, and a potential is applied between the DME and a reference electrode.

As the potential is scanned, reduction or oxidation of the analyte occurs at the DME surface, leading to a current that can be measured. The resulting polarogram (a plot of current vs. voltage) shows peaks or waves corresponding to the redox potentials of the analyte, which can be used to identify and quantify the species present in the solution.

Polarography is a sensitive and selective technique that has been widely used in fields such as environmental analysis, pharmaceuticals, and biochemistry. However, it has largely been replaced by more modern electrochemical techniques, such as cyclic voltammetry and differential pulse voltammetry, which offer higher sensitivity and better resolution of complex mixtures.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Reagent strips, also known as diagnostic or test strips, are narrow pieces of plastic material that have been impregnated with chemical reagents. They are used in the qualitative or semi-quantitative detection of various substances, such as glucose, proteins, ketones, blood, and white blood cells, in body fluids like urine or blood.

Reagent strips typically contain multiple pad areas, each with a different reagent that reacts to a specific substance. To perform the test, a small amount of the fluid is applied to the strip, and the reaction between the reagents and the target substance produces a visible color change. The resulting color can then be compared to a standardized color chart to determine the concentration or presence of the substance.

Reagent strips are widely used in point-of-care testing, providing quick and convenient results for healthcare professionals and patients alike. They are commonly used for monitoring conditions such as diabetes (urine or blood glucose levels), urinary tract infections (leukocytes and nitrites), and kidney function (protein and blood).

Flavin-Adenine Dinucleotide (FAD) is a coenzyme that plays a crucial role in various metabolic processes, particularly in the electron transport chain where it functions as an electron carrier in oxidation-reduction reactions. FAD is composed of a flavin moiety, riboflavin or vitamin B2, and adenine dinucleotide. It can exist in two forms: an oxidized form (FAD) and a reduced form (FADH2). The reduction of FAD to FADH2 involves the gain of two electrons and two protons, which is accompanied by a significant conformational change that allows FADH2 to donate its electrons to subsequent components in the electron transport chain, ultimately leading to the production of ATP, the main energy currency of the cell.

Glycosuria is a medical term that refers to the presence of glucose in the urine. Under normal circumstances, the kidneys are able to reabsorb all of the filtered glucose back into the bloodstream. However, when the blood glucose levels become excessively high, such as in uncontrolled diabetes mellitus, the kidneys may not be able to reabsorb all of the glucose, and some of it will spill over into the urine.

Glycosuria can also occur in other conditions that affect glucose metabolism or renal function, such as impaired kidney function, certain medications, pregnancy, and rare genetic disorders. It is important to note that glycosuria alone does not necessarily indicate diabetes, but it may be a sign of an underlying medical condition that requires further evaluation by a healthcare professional.

Horseradish peroxidase (HRP) is not a medical term, but a type of enzyme that is derived from the horseradish plant. In biological terms, HRP is defined as a heme-containing enzyme isolated from the roots of the horseradish plant (Armoracia rusticana). It is widely used in molecular biology and diagnostic applications due to its ability to catalyze various oxidative reactions, particularly in immunological techniques such as Western blotting and ELISA.

HRP catalyzes the conversion of hydrogen peroxide into water and oxygen, while simultaneously converting a variety of substrates into colored or fluorescent products that can be easily detected. This enzymatic activity makes HRP a valuable tool in detecting and quantifying specific biomolecules, such as proteins and nucleic acids, in biological samples.

Ferrocyanides are salts or complex ions containing the ferrocyanide ion (Fe(CN)2-4). The ferrocyanide ion is a stable, soluble, and brightly colored complex that contains iron in the +2 oxidation state coordinated to four cyanide ligands. Ferrocyanides are commonly used in various industrial applications such as water treatment, chemical synthesis, and photography due to their stability and reactivity. However, they can be toxic if ingested or inhaled in large quantities, so proper handling and disposal procedures should be followed.

Indicators and reagents are terms commonly used in the field of clinical chemistry and laboratory medicine. Here are their definitions:

1. Indicator: An indicator is a substance that changes its color or other physical properties in response to a chemical change, such as a change in pH, oxidation-reduction potential, or the presence of a particular ion or molecule. Indicators are often used in laboratory tests to monitor or signal the progress of a reaction or to indicate the end point of a titration. A familiar example is the use of phenolphthalein as a pH indicator in acid-base titrations, which turns pink in basic solutions and colorless in acidic solutions.

2. Reagent: A reagent is a substance that is added to a system (such as a sample or a reaction mixture) to bring about a chemical reaction, test for the presence or absence of a particular component, or measure the concentration of a specific analyte. Reagents are typically chemicals with well-defined and consistent properties, allowing them to be used reliably in analytical procedures. Examples of reagents include enzymes, antibodies, dyes, metal ions, and organic compounds. In laboratory settings, reagents are often prepared and standardized according to strict protocols to ensure their quality and performance in diagnostic tests and research applications.

Hexokinase is an enzyme that plays a crucial role in the initial step of glucose metabolism, which is the phosphorylation of glucose to form glucose-6-phosphate. This reaction is the first step in most glucose catabolic pathways, including glycolysis, pentose phosphate pathway, and glycogen synthesis.

Hexokinase has a high affinity for glucose, meaning it can bind and phosphorylate glucose even at low concentrations. This property makes hexokinase an important regulator of glucose metabolism in cells. There are four isoforms of hexokinase (I-IV) found in different tissues, with hexokinase IV (also known as glucokinase) being primarily expressed in the liver and pancreas.

In summary, hexokinase is a vital enzyme involved in glucose metabolism, catalyzing the conversion of glucose to glucose-6-phosphate, and playing a crucial role in regulating cellular energy homeostasis.

Flavoproteins are a type of protein molecule that contain noncovalently bound flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) as cofactors. These flavin cofactors play a crucial role in redox reactions, acting as electron carriers in various metabolic pathways such as cellular respiration and oxidative phosphorylation. Flavoproteins are involved in several biological processes, including the breakdown of fatty acids, amino acids, and carbohydrates, as well as the synthesis of steroids and other lipids. They can also function as enzymes that catalyze various redox reactions, such as oxidases, dehydrogenases, and reductases. Flavoproteins are widely distributed in nature and found in many organisms, from bacteria to humans.

Glucose Transporter Type 1 (GLUT1) is a specific type of protein called a glucose transporter, which is responsible for facilitating the transport of glucose across the blood-brain barrier and into the brain cells. It is encoded by the SLC2A1 gene and is primarily found in the endothelial cells of the blood-brain barrier, as well as in other tissues such as the erythrocytes (red blood cells), placenta, and kidney.

GLUT1 plays a critical role in maintaining normal glucose levels in the brain, as it is the main mechanism for glucose uptake into the brain. Disorders of GLUT1 can lead to impaired glucose transport, which can result in neurological symptoms such as seizures, developmental delay, and movement disorders. These disorders are known as GLUT1 deficiency syndromes.

I'm sorry for any confusion, but "Platinum" is not a medical term. Platinum is a chemical element with the symbol Pt and atomic number 78. It is a dense, malleable, ductile, highly unreactive, precious, silverish-white transition metal.

However, in the field of oncology, platinum-based compounds are used as chemotherapeutic drugs. These include:

1. Cisplatin: This is a platinum-containing drug that is used to treat various types of cancers such as testicular cancer, ovarian cancer, bladder cancer, and others. It works by forming crosslinks with the DNA of cancer cells, which disrupts their function and leads to cell death.

2. Carboplatin: This is another platinum-based chemotherapy drug that is used to treat various types of cancers such as ovarian cancer, lung cancer, and others. It is less toxic than cisplatin but has similar mechanisms of action.

3. Oxaliplatin: This is a third platinum-based chemotherapy drug that is used to treat colon cancer and rectal cancer. Like the other two drugs, it forms crosslinks with DNA and disrupts cell function leading to cell death.

These drugs are not made of pure platinum but contain platinum compounds that have been synthesized for medical use.

Magnesium silicates are a type of compound that consists of magnesium, silicon, and oxygen. They are often found in nature as minerals such as talc and serpentine. These compounds have a variety of uses, including as fillers in paper, paint, and rubber products, and as absorbents in cat litter.

In a medical context, magnesium silicates may be used as an antacid to neutralize stomach acid and relieve symptoms such as heartburn, indigestion, and upset stomach. They are also sometimes used as bulk-forming laxatives to treat constipation by absorbing water and swelling in the intestines, which helps to stimulate bowel movements.

It is important to note that some magnesium silicate compounds, such as talc, have been linked to health concerns when inhaled or ingested in large quantities. Therefore, they should be used as directed and under the guidance of a healthcare professional.

In the glucose oxidase assay, the glucose is first oxidized, catalyzed by glucose oxidase, to produce gluconate and hydrogen ... The glucose oxidase binds specifically to β-D-glucopyranose and does not act on α-D-glucose. It oxidises all of the glucose in ... "Glucose Oxidase: A much used and much loved enzyme in biosensors" at University of Paisley Glucose+Oxidase at the U.S. National ... Glucose oxidase catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone, which then hydrolyzes into gluconic acid. In ...
The factor was glucose oxidase. In the presence of glucose, the glucose oxidase produced hydrogen peroxide, which killed off ... "Detlev Müller discovers glucose oxidase". Archived from the original on 18 April 2018. Retrieved 13 June 2017. ... He is best known for discovering the enzyme, glucose oxidase, in 1925. In 1928, he was experimenting with the common fungus, ... Heller, Adam; Ulstrup, Jens (2021-05-11). "Detlev Müller's Discovery of Glucose Oxidase in 1925". Analytical Chemistry. 93 (18 ...
... trapping the enzyme glucose oxidase. The surrounding solution would end up containing the enzyme lipase B with the glucose ... The resulting glucose would cross the membrane, become oxidized, and the horseradish peroxidase would convert the sample ...
In a study by Oxenbøll et al., C. oxysporum catalyzed glucose oxidation by producing glucose oxidase, which it is mentioned in ... that the glucose oxidase helped protect against bacterial infection on the surface of fungi. The organism is also proven to be ... Oxenbøll, K; Si, J. Q; Aagaard, J (3 May 1995). "Alkaline glucose oxidase obtained from Cladosporium oxysporum". US Grant. ... It breaks down cellulose from dead herbaceous or plants, which is then further turned into glucose to Be used by the fungi ...
"Thermal stability of Penicillium adametzii glucose oxidase". Prikladnaia biokhimiia i mikrobiologiia. 37 (6): 678-86. PMID ...
Many glucose meters employ the oxidation of glucose to gluconolactone catalyzed by glucose oxidase (sometimes known as GOx). ... Glucose vs. plasma glucose: Glucose levels in plasma (one of the components of blood) are higher than glucose measurements in ... The glucose in the blood reacts with an enzyme electrode containing glucose oxidase (or dehydrogenase). The enzyme is ... This is important because home blood glucose meters measure the glucose in whole blood while most lab tests measure the glucose ...
Other work concerned enzymes such as "diaphorase", glucose oxidase, cytochrome oxidase and peroxidase. Much of Gibson's work ... Gibson, Q H; Massey, V; Swoboda, B E P J (1964). "Kinetics and mechanism of action of glucose oxidase". J. Biol. Chem. 239 (11 ... Gibson, Q H; Greenwood, C; Wharton, D C; Palmer, G (1965). "Reaction of cytochrome oxidase with cytochrome C". J. Biol. Chem. ... Brunori, M.; Gibson, Q.H. (1983). "Oxygen activation by cytochrome oxidase: A new spectral intermediate observed by flow-flash ...
"Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing". Analytical and Bioanalytical Chemistry. 380 (4): 606- ...
... glucose oxidase (P13006), used in the design of glucose biosensors, due to its high affinity for β-D-glucose. In the food ... "Nano-Encapsulation of Glucose Oxidase Dimer by Graphene". RSC Advances. 5 (18): 13570-78. doi:10.1039/C4RA16852F. S2CID ... Staiano M, Bazzicalupo P, Rossi M, D'Auria S (December 2005). "Glucose biosensors as models for the development of advanced ...
Commercially available glucose monitors rely on amperometric sensing of glucose by means of glucose oxidase, which oxidises ... which uses the enzyme glucose oxidase to break blood glucose down. In doing so it first oxidizes glucose and uses two electrons ... "Nano-Encapsulation of Glucose Oxidase Dimer by Graphene". RSC Advances. 5 (18): 13570-78. doi:10.1039/C4RA16852F. Daaboul, G.G ... Measured glucose data will be transmitted wirelessly out of the body within the MICS 402-405 MHz band as approved for medical ...
It is typically produced by the aerobic oxidation of glucose in the presence of the enzyme glucose oxidase. The conversion ... 18, V, 5, 11 Wong, Chun Ming; Wong, Kwun Hei; Chen, Xiao Dong (2008). "Glucose oxidase: Natural Occurrence, Function, ... A colorless solid, it is an oxidized derivative of glucose. ...
The aerobic oxidation of glucose in the presence of the enzyme glucose oxidase produces hydrogen peroxide. The conversion ... Wong, Chun Ming; Wong, Kwun Hei; Chen, Xiao Dong (2008). "Glucose oxidase: Natural Occurrence, Function, Properties and ... Hypoxanthine Xanthine oxidase H2O, O2 H2O2 Xanthine Xanthine oxidase H2O, O2 H2O2 Uric acid The degradation of guanosine ... and the reaction is catalyzed by the enzyme xanthine oxidase: ...
CHOD = cholesterol oxidase GOD = glucose oxidase GPO = glycerol-3-phosphate oxidase PAP = phenol + aminophenazone (in some ... water Glucose + oxygen + water --(enzyme glucose oxidase)--> gluconate + hydrogen peroxide Hydrogen peroxide + ABTS --(enzyme ... Cholesterol + oxygen --(enzyme cholesterol oxidase)--> cholestenone + hydrogen peroxide Hydrogen peroxide + 4-aminophenazone + ... enzyme glycerol-3-phosphate oxidase) --> dihydroxyacetone phosphate + hydrogen peroxide Hydrogen peroxide + 4-aminophenazone + ...
Glucose oxidase-like gold nanoparticles combined with cyclodextran were used for chiral catalysis. An artificial binuclear ... Glucose oxidase and iron oxide nanozymes were encapsulated within multi-compartmental hydrogels for incompatible tandem ... A Pd12 coordination cage as a photoregulated oxidase-like nanozyme was developed. An NADPH oxidase-like nanozyme was developed ... with glucose oxidase (GOx) in sub-micron proximity, providing a fast and efficient enzyme cascade reported as monitoring ...
... is typically produced by the aerobic oxidation of glucose in the presence of the enzyme glucose oxidase. The ... Wong, Chun Ming; Wong, Kwun Hei; Chen, Xiao Dong (2008). "Glucose oxidase: Natural Occurrence, Function, Properties and ... Glucose, Rohrzucker, Levulose, Sorbin, Phloroglucin.)" [[Contribution] to our knowledge of some types of sugars: glucose, ... Boutroux, L. (1880). "Sur une fermentation nouvelle du glucose" [On a new fermentation [product] of glucose]. Comptes Rendus de ...
"Reengineered glucose oxidase for amperometric glucose determination in diabetes analytics". Biosens. Bioelectron. 50: 84-90. ... glucose oxidase for analytical application, phytase with increased thermostability and monooxygenase with improved catalytic ...
For example , the immobilization of glucose oxidase on calcium alginate gel beads can be used in a bioreactor. The resulting ... Examples include entrapment of enzymes such as glucose oxidase in gel column for use as a bioreactor. Important characteristic ... "Production of gluconic acid with immobilized glucose oxidase in airlift reactors". Chemical Engineering Science. 52 (21-22): ... Kinetic studies of Immobilized glucose oxidase". Biotechnology and Bioengineering. 16 (2): 159-168. doi:10.1002/bit.260160202. ...
... bees use the enzyme glucose oxidase, stored in their hypopharyngeal glands. Glucose oxidase works to ... Burgett, D. Michael (January 9, 1974). "Glucose Oxidase: A Food Protective Mechanism in Social Hymenoptera" (PDF). Annals of ...
Biosensors/diagnostics, e.g. glucose oxidase and cholesterol oxidase biosensors. Delivery of proteins as therapeutic agents or ...
The three primary enzymes in Biotène are[were? no longer, per the above] Glucose Oxidase, Lactoperoxidase, and Lysozyme. ... and glucose oxidase. People with xerostomia (dry mouth) may use Biotène to reduce the rate of recurrence of dental plaque. ... and prior to the GSK acquisition it also contained enzymes including glucose oxidase, lactoferrin, lactoperoxidase and lysozyme ...
Now, however, the membrane is impregnated with immobilized glucose oxidase (GOx). The GOx will consume some of the oxygen as it ... leaving as the only variable the oxygen and glucose concentrations on the analyte-side of the glucose membrane, which is the ... The Clark oxygen electrode laid the basis for the first glucose biosensor (in fact the first biosensor of any type), invented ... The rate of reaction current is limited by the diffusion of both glucose and oxygen. This diffusion can be well characterized ...
GNP-glucose oxidase monolayer electrode was constructed use these two methods. The Au NP allowed more freedom in the enzyme's ... These ribbons are very flexible and can bend with angles larger than 90°. When glucose is replaced by cyclodextrin (a glucose ... In another method using ultrasound, the reaction of an aqueous solution of HAuCl4 with glucose, the reducing agents are ... Large AuNPs conjugated with biotin, cysteine, citrate, and glucose were not toxic in human leukemia cells (K562) for ...
Petruccioli, M.; Federici, F. (1993). "Glucose oxidase production by Penicillium variabile P16: Effect of medium composition". ... "Expression of Penicillium variabile P16 glucose oxidase gene in Pichia pastoris and characterization of the recombinant enzyme ...
These glucose sensitive hydrogels are modified with the enzyme glucose oxidase. In the presence of glucose, the glucose oxidase ... An example of this would be hydrogels that release insulin in the presence of high glucose levels in the bloodstream. ...
"Glucose-sensitive membranes containing glucose oxidase: Activity, swelling, and permeability studies". Journal of Biomedical ... The major focus has been the development of a non-invasive continuous detection of glucose. The first clinical study on ... Since, Kost also proposed a novel approach for a glucose flux continuous biosensor and noninvasive detection of amniotic fluid ... In addition to his studies on responsive controlled release systems: pH sensitive, glucose sensitive and calcium sensitive drug ...
Studies of Enzyme-Mediator Kinetics for Membrane and Surface Immobilized Glucose Oxidase". Anal. Chem. 64 (17): 1795-1804. doi: ...
... and urea-induced unfolding of the dimeric enzyme glucose oxidase". Biochemistry. 41 (11): 3819-27. doi:10.1021/bi0116700. PMID ...
The extract has also shown significant inhibition against glucose oxidase-mediated inflammation. The observations have ...
Recently, pyranose oxidase has been gaining on popularity within biosensors. Unlike glucose oxidase, it can produce higher ... Other names in common use include glucose 2-oxidase, and pyranose-2-oxidase. This enzyme participates in pentose phosphate ... In enzymology, a pyranose oxidase (EC is an enzyme that catalyzes the chemical reaction D-glucose + O2 ⇌ {\ ... whereas its two products are 2-dehydro-D-glucose and H2O2. Pyranose oxidase is able to oxidize D-xylose, L-sorbose, D-galactose ...
Roth JP, Klinman JP (January 2003). "Catalysis of electron transfer during activation of O2 by the flavoprotein glucose oxidase ... Leys D, Basran J, Scrutton NS (August 2003). "Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase". ...
In the glucose oxidase assay, the glucose is first oxidized, catalyzed by glucose oxidase, to produce gluconate and hydrogen ... The glucose oxidase binds specifically to β-D-glucopyranose and does not act on α-D-glucose. It oxidises all of the glucose in ... "Glucose Oxidase: A much used and much loved enzyme in biosensors" at University of Paisley Glucose+Oxidase at the U.S. National ... Glucose oxidase catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone, which then hydrolyzes into gluconic acid. In ...
What is the العربية for glucose oxidase? Translation of 'glucose oxidase' to العربية ... glucose oxidase - ترجمة إلى العربية. CLASS OF ENZYMES Glucose Oxidase Enzyme; GOx; E1102; Notatin; Penicillin A; Penicillin B; ... Glucose oxidase. The glucose oxidase enzyme (GOx or GOD) also known as notatin (EC number is an oxidoreductase that ... Glucose oxidase is widely used for the determination of free glucose in body fluids (medical testing), in vegetal raw material ...
Glucose Oxidase) (65C-CE0203) 5mG.. ...
Chinas leading glucose oxidase fermentation product, with strict quality control production d gluconic acid factories, ... producing high quality Glucose Oxidase And Peroxidase products. ... 1. Role of glucose oxidase in wheat flour. Glucose oxidase can ... High quality Peroxidase Glucose Oxidase Gox Fermentation Production D Gluconic Acid from China, ... Other uses of glucose oxidase include the removal of oxygen from food packaging and removal of D-glucose from egg white to ...
Glucose Fermenting, Oxidase Pos, Curved Gram Neg Bacilli. N/a. Author: jamguyette Cards: 26 Subject: Microbiology Level: ...
Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid ... N2 - Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic ... AB - Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic ... abstract = "Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and ...
keywords = "glucose oxidase, glucose sensor, graphene, molecular dynamics, protein design",. author = "Inchul Baek and Hyunsung ... Glucose oxidase (GOx) is one of the most widely investigated enzymes in the field of bioelectrochemistry. It is mainly used for ... N2 - Glucose oxidase (GOx) is one of the most widely investigated enzymes in the field of bioelectrochemistry. It is mainly ... AB - Glucose oxidase (GOx) is one of the most widely investigated enzymes in the field of bioelectrochemistry. It is mainly ...
The aim of this study was in silico and in vivo analysis of SPs effect on the production of recombinant glucose oxidase (GOX) ... In silico and in vivo analysis of signal peptides effect on recombinant glucose oxidase production in nonconventional yeast ... In silico and in vivo analysis of signal peptides effect on recombinant glucose oxidase pr ... Glucosa Oxidasa/biosíntesis; Glucosa Oxidasa/genética; Señales de Clasificación de Proteína/fisiología; Proteínas Recombinantes ...
Senel, M.; Nergiz, C. Novel amperometric glucose biosensor based on covalent immobilization of glucose oxidase on poly(pyrrole ... glucose oxidase. Gold nanocomposite/poly(pyrrole propylic acid). Graphene/nafion Film. 50 mmol L-1 30 mmol L-1 [91]. [92]. ... but also due to the stability of glucose oxidase (GOX).. The stability of enzymatic biosensors is important for the success of ... lactate oxidase. Carbon screen-printed/mesoporous silica. Carbon screen-printed/polysulfone-carbon nanotubes. 18.3 μmol L-1 1.5 ...
Treatment with glucose oxidase (GO) significantly stimulated the formation of ROS and increased the production of MDA, as ... In the present study, GO reacted with glucose in the culture media resulting in the generation of glucuronic acid and H2O2. ... As a marker of oxidative stress, GO may react with glucose in the culture media and subsequently promote the generation of ... Bisbal C, Lambert K and Avignion A: Antioxidants and glucose metabolism disorders. Curr Opin Clin Nutr Metab Care. 13:439-446. ...
result sql = glucose oxidase. glucose oxidase 9. char = A;code = 65. char = c;code = 99. char = e;code = 101. char = t;code = ... result sql = Glucose. Glucose 22. char = M;code = 77. char = e;code = 101. char = t;code = 116. char = h;code = 104. char = y; ... start str = glucose oxidase. sql str = glucose oxidase. Bromide ion and glucose oxidase ...
Fiedurek J (1998) Effect of osmotic stress on glucose oxidase production and secretion by Aspergillus niger. J Basic Microbiol ... 2015) reported that for T. atroviride IMI 206040 cultivation in the control run about 78 % of the initial glucose was consumed ... So, from their results, no correlation between glucose consumption and pellet size could be established. ...
Moreover, levels of plasma glucose, triglycerides, and cholesterol, plasma leptin and resistin, liver enzymes, renal function ... Hydrogen peroxide in honey is produced from the oxidation of glucose by glucose oxidase enzyme. ... Glucose, triglyceride, and cholesterol of rats in HFD group were significantly higher compared to the control rats (Table 3). ... N. Yaghoobi, N. Al-Waili, M. Ghayour-Mobarhan et al., "Natural honey and cardiovascular risk factors; effects on blood glucose ...
... oxygen was enzymatically removed by glucose oxidase treatment. The analyzed liposome samples were contained in a square (10 mm ... On the day of the assay, the cells were washed with XF Media (XF Media (Seahorse), glucose (4.5 g/1 L), 1 mM sodium pyruvate, 1 ... D-glucose, glutamic acid, and D-galactose were obtained from Thermo Scientific. ...
The isolate was motile, catalase positive, oxidase negative, and it fermented glucose and lactose. Reactions for indole, urea, ...
BakeZyme® Go Pure is a glucose oxidase which allows for the dough to become elastic. ... Most common glucose oxidases on the market originate from Aspergillus sp. DSM has developed a new glucose oxidase originating ... The use of a glucose oxidase during the dough making process is well known within the bakery industry. ... maintaining its ability to stretch and creates new opportunities to use glucose oxidase as a tool for replacing chemical ...
The glucose oxidase method was used to assess fasting blood glucose (FBG). Routine enzymatic techniques were used to evaluate ... An animal study in rats showed that NRG-1 injection promoted glucose tolerance following an oral glucose load.9 Another study ... Acute administration of NRG-1 was found to reduce plasma glucose in experimental mice and pigs, via enhancing glucose uptake by ... Several mechanisms for this effect on glucose disposal have been suggested. NRG-1 was reported to influence glucose transporter ...
Wet lab - Comparison between glucose oxidase enzymatic assay and 3,5-dinitrosalicylic acid (DNS) assay for reducing sugars ...
The new feed enzyme - Glucose Oxidase. It is well known that in the current floor pen with deep litter system, day old broiler ...
7] It consists of yellow pigment-producing, nonmotile, catalase-positive, oxidase-positive, non-glucose-fermenting, gram- ...
... glucose oxidase) for glycosuria. Therefore, it is recommended that glucose tests based on enzymatic glucose oxidase reactions ... with glucose 5% solution, glucose 5% or 10% solution, Ringer lactate solution, Ringer lactate with glucose 5% solution, Sodium ... Cephalosporin antibiotics may produce a false-positive reaction for glucose in the urine with copper reduction tests ( ...
Possible false-positive with tests based on cupric sulfate reagent and false-negative with tests that use glucose oxidase ...
It is recommended that glucose tests based on enzymatic glucose oxidase reactions (such as Clinistix® or Tes-Tape®) be used. ... The administration of cefdinir may result in a false-positive reaction for glucose in urine using Clinitest®, Benedicts ... false-positive test for urinary glucose, neutropenia, pancytopenia, and agranulocytosis. Pseudomembranous colitis symptoms may ...
Biofuel Cell Based on a Complex between Glucose Oxidase and a Plasma-Polymerized Film Containing a Redox Site Hitoshi MUGURUMA ...
Glucose Oxidase Immobilized in Alginate/Layered Double Hydroxides Hybrid Membrane and Its Biosensing Application ...
They fabricated a glucose biosensor similar to Michigan style neural electrodes. Glucose oxidase, an enzyme for the specific ... Toward that end, the team successfully incorporated bioactive molecules such as laminin and glucose oxidase into the OS ... The biosensor offered a highly sensitive glucose sensing platform with nearly 10-fold higher sensitivity compared to previous ... recognition of glucose, was encapsulated within the solidified OS composite microelectrodes via the MPL process. ...
Glucose (Hexokinase)†. Glucose (Oxidase)†. HDL Cholesterol. Iron. Lactate. Lactate Dehydrogenase (L-P). Lactate Dehydrogenase ( ...
Capillary blood was sampled for the determination of plasma glucose concentrations (glucose oxidase method; EBIOS; Eppendorf, ... Normal glucose tolerance . Type 1 diabetes . Low . Intermediate . High . Significance (P value) . Low . Intermediate . High . ... Normal glucose tolerance . Type 1 diabetes . Low . Intermediate . High . Significance (P value) . Low . Intermediate . High . ... Day-to-Day Variations in Fasting Plasma Glucose Do Not Influence Gastric Emptying in Subjects With Type 1 Diabetes Lea Aigner; ...
  • The glucose oxidase enzyme (GOx or GOD) also known as notatin (EC number is an oxidoreductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. (
  • Several species of fungi and insects synthesize glucose oxidase, which produces hydrogen peroxide, which kills bacteria. (
  • Early experiments showed that notatin exhibits in vitro antibacterial activity (in the presence of glucose) due to hydrogen peroxide formation. (
  • citation needed] In the glucose oxidase assay, the glucose is first oxidized, catalyzed by glucose oxidase, to produce gluconate and hydrogen peroxide. (
  • 1. Scientists believe its healing properties are due to the presence of the enzyme glucose oxidase , which produces hydrogen peroxide - an antiseptic - and its high sugar concentration, which inhibits bacterial growth. (
  • Glucose oxidase can be converted into glucose by the presence of oxygen in the presence of oxygen, and hydrogen peroxide. (
  • Oxidative stress in skin of B6C3F1 mice of both sexes was generated by intradermal injection of the hydrogen peroxide (H2O2) -producing enzyme, glucose oxidase with polyethylene glycol (GOD+PEG). (
  • This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present. (
  • GOx is a glucose oxidising enzyme with a molecular weight of 160 kDa. (
  • The direct electrochemistry of glucose oxidase (GOD) was revealed at a carbon nanotube (CNT)-modified glassy carbon electrode, where the enzyme was immobilized with a chitosan film containing gold nanoparticles. (
  • Glucose oxidase [GOx-(PT-PEO NH2 )] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid residues on the enzyme surface via poly(ethylene oxide) (PEO) spacers of different molecular weights. (
  • It is mainly used for the detection of glucose in solutions and enzyme-based biofuel cells. (
  • In the present study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. (
  • [ 1 ] Two of the patients had almost total deficiency of hepatic glucose-6-phosphatase, whereas the remaining 4 had normal enzyme activity. (
  • Glucose oxidase catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone, which then hydrolyzes into gluconic acid. (
  • and glucose oxidase (GOX), regulating gluconic acid (GLA) accumulation and acidification of the host tissue during fungal growth. (
  • The isolate was motile, catalase positive, oxidase negative, and it fermented glucose and lactose. (
  • Glucose oxidase is widely used coupled to peroxidase reaction that visualizes colorimetrically the formed H2O2, for the determination of free glucose in sera or blood plasma for diagnostics, using spectrometric assays manually or with automated procedures, and even point-of-use rapid assays. (
  • Sociodemographic and diagnosis variables (presence of dental calculus and periodontal status) were considered to measure salivary concentrations of glucose (by the glucose oxidase/peroxidase method, amylase (by the colorimetric test), urea (by the amount of indophenol), total protein (by the Bradford method) and albumin (by the nephelometric method). (
  • Glucose oxidase (GOx) is one of the most widely investigated enzymes in the field of bioelectrochemistry. (
  • Blood samles were assayed for plasma glucose, insulin, growth hormone, adrenaline and noradernaline in the fasting state and 10, 30, 60, 90, 120 and 180 minutes after the end of smoking by the glucose oxidase method for glucose, radioimmunoassay for insulin and growth hormone, and flourometry for catecholamines. (
  • The results of the present study showed significant elevation of plasma glucose after both types of smoking, with peak glucose response occurring earlier after Goza smoking. (
  • Diabetes was defined by the presence of fasting plasma glucose 126 mg/dl or the use of oral hypoglycemic agents or insulin. (
  • Serum glucose values are 1.15% lower than plasma glucose values. (
  • Morning fasting plasma glucose values are higher than afternoon glucose levels. (
  • In heparinized plasma, glucose concentrations are 5% lower than plasma. (
  • Biotin reagent (Glucose Oxidase) (65C-CE0203) 5mG. (
  • Similar assays allows the monitoring of glucose levels in fermentation, bioreactors, and to control glucose in vegetal raw material and food products. (
  • In the presence of dissolved oxygen, the reduction peak current decreased gradually with the addition of glucose, which could be used for reagentless detection of glucose with a linear range from 0.04 to 1.0 mM. (
  • Glucose oxidase is widely used for the determination of free glucose in body fluids (medical testing), in vegetal raw material, and in the food industry. (
  • A major use of glucose oxidase has been in the determination of free glucose in body fluids, food and agricultural products. (
  • Because free glucose is the product of the hepatic glucose-6-phosphatase reaction, either type leads to accumulation of liver glycogen, accompanied by fasting hypoglycemia . (
  • The liver loses its capacity as a glucose-homeostatic organ because of a fundamental inability to release free glucose. (
  • This is the technology behind the disposable glucose sensor strips used by diabetics to monitor serum glucose levels. (
  • For serum glucose, a red-top tube can be used. (
  • Objective: To assess the prevalence of DM and impaired glucose tolerance (pre-diabetes) among newly diagnosed tuberculosis cases in Ijebu-Ode Local Government Area of Ogun State, Nigeria. (
  • It involves a set of three or more alterations such as overweight or obesity and disturbance in glucose metabolism and insulin, along with hypertension, dyslipidemia, and other abnormalities of importance that are related to its development and are grouped in different profiles, such as liver, pancreatic, and cardiovascular functions [ 1 - 4 ]. (
  • Of the 10 GLUT receptors, GLUT-4 receptors are present in muscle and adipose tissues and require insulin for glucose transport. (
  • It is also used as a food preservative to help remove oxygen and glucose from food when packaged such as dry egg powder to prevent unwanted browning and undesired taste. (
  • Other uses of glucose oxidase include the removal of oxygen from food packaging and removal of D-glucose from egg white to prevent browning. (
  • It oxidises all of the glucose in solution because the equilibrium between the α and β anomers is driven towards the β side as it is consumed in the reaction. (
  • Enzymatic glucose biosensors use an electrode instead of O2 to take up the electrons needed to oxidize glucose and produce an electronic current in proportion to glucose concentration. (
  • Glucose is measured by enzymatic methods. (
  • The proposed glucose biosensor exhibited high sensitivity, good stability and reproducibility, and was also insensitive to common interferences such as ascorbic and uric acid. (
  • In this study, we propose a method to improve the stability of GOx and secure its immobility on the graphene sheet and its glucose-binding affinity by single-point mutation of GOx using molecular dynamics simulations. (
  • Most common glucose oxidases on the market originate from Aspergillus sp . (
  • In the production of noodles, glucose oxidase is a good protein network structure, which can increase the strength of the noodles. (
  • The use of a glucose oxidase during the dough making process is well known within the bakery industry. (
  • ORCID: 0000-0001-6953-3655 and Smyth, Malcolm R. (2006) Reagentless glucose biosensor based on the direct electrochemistry of glucose oxidase on carbon nanotube-modified electrodes. (
  • Methods for bonding electron- transfer relays to glucose oxidase and D-Amino-Acid oxidase. (
  • Glucose is initially used by glycolysis and is converted to pyruvate. (
  • However, glucose-6-phosphate is also the substrate for glycolysis and produces lactate. (
  • Preparation of Iodine-iodide-molybdate solution to determine glucose level by glucose oxidase method. (
  • The patients were selected from four health facilities and were screened for elevated Fasting Blood Glucose levels using a laboratory spectrophotometer (glucose oxidase method). (
  • Blood glucose determination: plasma or serum? (
  • BakeZyme® Go Pure allows for the dough to become elastic, maintaining its ability to stretch and creates new opportunities to use glucose oxidase as a tool for replacing chemical oxidizers (such as ADA or Bromate) or in applications such as frozen dough. (
  • They grow poorly on MacConkey agar and are considered glucose oxidizers. (
  • In silico and in vivo analysis of signal peptides effect on recombinant glucose oxidase production in nonconventional yeast Yarrowia lipolytica. (
  • The aim of this study was in silico and in vivo analysis of SPs effect on the production of recombinant glucose oxidase (GOX) in Yarrowia lipolytica . (
  • Glucose is primarily stored as glycogen in muscles and liver. (
  • Glucose measurements are used in the diagnosis and treatment of pancreatic islet cell carcinoma and of carbohydrate metabolism disorders, including diabetes mellitus, neonatal hypoglycemia, and idiopathic hypoglycemia. (
  • For gestational diabetes testing, parameters are 1 hour after 50 g of glucose and 2 hours after 100 g of glucose. (
  • noun Medicine monoamine oxidase inhibitor, a type of antidepressant drug. (
  • Eleven (11.0%) had elevated blood glucose levels suggestive of DM, while 20 (20.0%) had impaired fasting blood glucose levels. (
  • For fasting glucose testing, collect the blood sample in the morning after an overnight or 8-hour fast. (
  • For postprandial glucose testing, collect the blood sample 2 hours after a regular meal. (
  • For oral glucose tolerance testing, after oral intake of 75 g of glucose, collect blood samples at 1 hour and 2 hours. (
  • The usual homeostatic mechanism cannot halt the rapid drop in blood glucose levels that normally occurs during the first several hours after birth (reflecting consumption of maternal glucose), and the decrease continues. (
  • This decrease in circulating glucose can be precipitous, resulting in no measurable blood level. (
  • Hyperuricemia can reach levels that require use of xanthine oxidase inhibitors to prevent nephrolithiasis. (
  • A very high WBC count can lead to a false low glucose level. (
  • Glucose is a monosaccharide and is a primary metabolite for energy production in the body. (
  • At pH 7, glucose exists in solution in cyclic hemiacetal form as 63.6% β-D-glucopyranose and 36.4% α-D-glucopyranose, the proportion of linear and furanose form being negligible. (