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Urate Oxidase

Urate oxidase is an enzyme that catalyzes the oxidation of uric acid to allantoin, a more soluble compound that can be more easily excreted.
It plays a key role in purine metabolism and is found in many organisms, including humans, where its deficiency can lead to hyperuricemia and related conditions such as gout.
Urate oxidase is an important target for research and therapeutic interventions, and the PubCompare.ai platform can help optimzie research protocols to ensure reproducibility and identify the most effective methods for advancing this field of study.

Most cited protocols related to «Urate Oxidase»

Blood samples were obtained by peripheral venous puncture, immediately centrifuged at 3000 × g for 10 min, and then stored at −80 °C until analysis. Total cholesterol, triglyceride, high-density lipoprotein (HDL), low-density lipoprotein (LDL), serum creatinine, and blood glucose were measured using an automatic biochemical analyzer (model 7600; Hitachi, Ltd., Tokyo, Japan). Serum UA level was measured with a Hitachi clinical chemistry analyzer with the uricase HMMPS method. Five samples were used to evaluate the intra-assay and inter-assay coefficients of variation (CV), which ranged from 2.3% to 4.5% and from 3.2% to 6.4%, respectively. Estimated glomerular filtration ratio (eGFR) was calculated using the Modification of Diet in Renal Disease formula24 (link). Hyperuricemia was defined as serum UA level of ≥420 μmol/L for men and ≥360 μmol/L for women.
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Publication 2018
Biological Assay BLOOD Blood Glucose Cholesterol Creatinine Dietary Modification Filtration High Density Lipoproteins Hyperuricemia Kidney Diseases Kidney Glomerulus Low-Density Lipoproteins Serum Triglycerides Urate Oxidase Venipuncture Woman
In the infinite dilution limit, assuming that the macromolecule has one preferential conformation, the scattering intensity of a sample solution containing the macromolecule is proportional to the scattering intensity of a single macromolecule of scattering density  (r), surrounded by a solvent of average electron density . The scattering intensity of this macromolecule at a given value of the wavevector norm q is the spherical average of the scattering intensity on the sphere of radius q in reciprocal space (Equation 1).

where A is the excess form factor of the system and are respectively the form factor of the solute in vacuo and of the solvent-excluded-volume. is the excess form factor of the hydration shell.
We perform the spherical averaging using the cubature formulae (30 ). Following the effective-atomic-scattering-form-factor method (25 ), the solute and the solvent-excluded-volume's form factors are computed as a sum over all N non-Hydrogen atoms of the solute (Equations 2 and 3).


where fj is the atomic form factor in vacuo (19 ), computed as a sum of a constant and four gaussians whose parameters depend on the atom type, is the solvent volume displaced by atom j. is an overall expansion factor, as defined in (19 ), with C1 being the ratio of the adjusted and computed average atomic radii (default value = 1.0).
Programs such as AquaSol (28 (link)) [or 3D-RISM/Amber (29 )] compute solvent density maps around the solute, based on the physical interactions within the system. The method used in AquaSol is based on the Poisson–Boltzmann formalism, where the solvent is no longer described as a continuum dielectric medium but rather as an assembly of self-orienting dipoles of variable density on a grid. It was shown that the resulting water distribution is in good agreement with experimental data and with the chemical nature of the atoms exposed to the solvent, both at the atomic and residue-level (26 (link)). These maps are typically cubic grids of given size and resolution (a), where each grid point r is associated to a given density value . Basically, in such maps, one expects a density of 0 inside the solute, and 1 (in units of bulk density ) in the bulk region of the solvent, i.e. far from the solute. At the boundary between the solute and bulk region, the density is determined by the physico–chemical nature of the environment.
We compute the form factor for the hydration shell as in Equation 4.

The sum runs over all points with nonzero density. In practice, to reduce computation time, grid points with a density close to 1 (i.e. typically within 1.10−4) are removed from the sum. On Urate Oxidase (example mentioned below), allowing a tolerance of 1.10−6 slowed down the computation by a factor of three and did not affect the resulting profile: the same fitting parameters were found, and the goodness-of-fit (cf Equation 6) was similar (1.688 versus 1.691).
Besides the solute and solvent, another possible contributor to the SAXS profile is the ion atmosphere surrounding the solute. AquaSol (28 (link)) computes the density maps of free cations and anions, and, in principle, these maps could be used to compute the excess form factors of ions. However, at physiological concentrations (200 mM NaCl) the ratio of the fugacities of ions and water is < 0.5%. At this stage, the contribution of ions was not implemented into AquaSAXS, except in the form of explicitly bound and fixed ions. Nevertheless, the presence of free ions can indirectly affect the solvent density in the hydration shell (screening effect), so the user is prompted for the ionic strength of the solution.
Alternatively, the hydration shell's form factor can be computed as in FoXS (20 (link)), following Equation 5.

where is the fraction of solvent accessible surface of the atom j (31 (link)) and is the water form factor. is a scale factor used to adjust the hydration shell's contribution (default value = 1.0).
The computed profile is fitted to a given experimental SAXS profile (with experimental error ) by minimizing the goodness-of-fit function with respect to three adjustable parameters: C1, C2 and C (Equation 6).

C1 and C2 values are scanned within a given range ( , and ), in steps of 0.0055, 0.014 and 0.04, resp., and for each pair, a linear-least-squares minimization is performed to adjust the scaling constant C. The pair leading to the minimal χ is kept to compute the returned profile.
Publication 2011
Amber Anions Aquasol A Atmosphere Cations Cuboid Bone Dietary Fiber Electrons factor A Hydrogen Immune Tolerance Ions Microtubule-Associated Proteins Physical Examination Radius Respiratory Rate Sodium Chloride Solvents Technique, Dilution Urate Oxidase
Acridine orange, ATP, bafilomycin A1, cytochalasin D, LPS, PMA, poly(deoxyadenylic-thymidylic) acid sodium salt (dAdT), sucrose and zymosan were purchased from Sigma-Aldrich (St. Louis, MO). CA-074-Me and PEG 1000 were purchased from Calbiochem (Gibbstown, NJ). DQ-ovalbumin, A647-conjugated dextran, A647-conjugated choleratoxin B, lysosensor green and Hoechst stain were obtained from Molecular Probes, Invitrogen (Carlsbad, CA). Alum (Imject Alum Adjuvant, mixture of aluminum hydroxide and magnesium hydroxide) was purchased from Pierce (Rockford, IL). Leu-Leu-OMe·HCl was purchased from Chem-Impex International (Wood Dale, IL). Uricase (Elitek™) was purchased from Sanofi-Aventis (Bridgewater, NJ).
Silica crystals (MIN-U-SIL-15) were kindly provided by U.S. Silica Company (Berkeley Springs, WV). Throughout the study, a polydispersed preparation of silica crystals of up to 15 µm were used. MSU crystals were prepared as previously described37 (link).
Publication 2008
Acridine Orange alum, potassium bafilomycin A1 CA 074 Choleragenoid Cytochalasin D Dextran Elitek Hydroxide, Aluminum leucyl-leucine-methyl ester Magnesium Hydroxide Molecular Probes Natural Springs Ovalbumin Poly A polyethylene glycol 1000 Silicon Dioxide Sodium Sodium Chloride Stains Sucrose Thymidine Monophosphate Urate Oxidase Zymosan
A gene encoding urate oxidase (UO, VectorBase AAEL002194) was previously studied in A. aegypti[13] (link). In this report, a putative ortholog of the mosquito arginase gene (AR, VectorBase AAEL002675) was identified by BLAST searches using fruit fly arginase (FBpp0070083-PA as a query [21] (link)). The arginase gene in A. aegypti is a single copy gene. It encodes a protein of 349 residues and shares 85%, 43% and 54% identity to Anopheles gambiae, D. melanogaster, and Bombyx mori, respectively.
UO, AR and firefly luciferase (FL, GenBank accession number U47295) gene-specific primers flanked with T7 promoter sequence (Table 1) were used to PCR amplify DNA from mosquito cDNA and pGL3 vector (Promega, Madison, WI). Double-stranded RNA (dsRNA) covers approximately the first half of the coding sequence of UO or AR genes, and the target region corresponds to the catalytic domain of each protein. The dsRNA was prepared as described previously [17] (link). Newly-eclosed females were injected with 500 ng of dsRNA using a Nanoject II microinjector (Drummond Scientific Company, Broomall, PA) [13] (link). Females were fed with a blood meal 4 days later.
The FB and MT were dissected from individual mosquitoes at 24 h and 48 h after blood feeding. Total RNA was extracted using TRIzol reagent (Life Technologies, Carlsbad, CA) and reverse transcribed using oligo-(dT)20 primer and reverse transcriptase (Promega, Madison, WI). The cDNA was then used as a template for qRT-PCR assays using gene-specific primers (Table 1). UO and AR knockdown efficiency, as well as the relative mRNA level of several other genes involved in nitrogen metabolism in A. aegypti were analyzed by qRT-PCR. Briefly, qRT-PCR was performed with PerfeCTa SYBR Green FastMix, ROX (Quanta BioSciences, Gaithersburg, MD) and a final primer concentration of 200 nM using Applied Biosystems 7300 Real-Time PCR System (Life Technologies, Carlsbad, CA) and the following PCR conditions: 95°C for 2 minutes followed by 40 cycles of 95°C for 10 seconds and 60°C for 30 seconds. The PCR efficiency of a primer set for each gene were verified by performing a dilution series experiment with a corresponding cloned plasmid DNA. Relative level of expression for each gene was calculated using the ΔΔCT quantification method [24] (link). Ribosomal protein S7 transcript levels were used as an internal control for normalization of mRNA yields in all samples. The knockdown efficiency was determined as previously described [13] (link).
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Publication 2013
Anopheles gambiae Arginase Biological Assay BLOOD Bombyx mori Catalysis Catalytic Domain Cloning Vectors Culicidae DNA, A-Form DNA, Complementary Drosophila Drosophila melanogaster Females Genes Genes, vif Luciferases, Firefly Metabolism Neoplasm Metastasis Nitrogen Oligonucleotide Primers Oligonucleotides Open Reading Frames Paragangliomas 3 Plasmids Promega Protein Domain Proteins ribosomal protein S7 RNA, Double-Stranded RNA, Messenger RNA-Directed DNA Polymerase Staphylococcal Protein A SYBR Green I Technique, Dilution trizol Urate Oxidase
All lines were maintained on a standard Drosophila diet at 22°C, 55% humidity on a 12∶12 h light∶dark photoperiod. Wild-type flies were obtained from a Canton-S (CS) stock. In order to drive cell- and tissue-specific gene expression of gene(s) of choice in vivo, the GAL4/UAS system was used, in which cell- or tissue-specific GAL4 ‘drivers’ enable binary expression of genes cloned downstream of the GAL4-binding Upstream Activating Sequence [15] (link). Thus, for intact tubules, principal cell-specific expression can be driven using either c42-GAL4 [16] (link) or Urate-Oxidase-GAL4 [17] (link) drivers in an otherwise normal fly. To assess in vivo calcium signals, doubly homozygous c42-GAL4>UAS-apoaequorincyto (c42aeq) flies were used, which specifically express the apoaequorin luminescent calcium reporter in the cytosol of the principal cells of the tubule main segment (upon which the diuretic neuropeptide capa-1 acts) [18] (link). The ubiquitous actin-GAL4 and the UAS-GFP lines were obtained from the Bloomington Stock Center (Bloomington, IN). To assess the impact of capaR and capaR RNAi on calcium signaling in vivo, lines were crossed to the doubly homozygous c42aeq flies. The ORF of the capaR (CG14575) was amplified from whole fly cDNA as template using the primers 5′-CGCGGCCGCATGAATTCATCGACCG-3′ and 5′-GCGGTACCTTAAATACAAGTCTC-3′ and cloned into the pUAST vector. To generate construct for heritable RNA interference (RNAi) of the capaR gene, an inverted repeat of a 615 base pair fragment was generated by PCR using the primers 5′-GCACTCTAGAACAAGGCAGTTTTGATAAC-3′ and 5′-GCACTCTAGAGTTCGAGATCGAATCTTGGC-3, and cloned as a tail-tail inverted repeat flanking the white intron into the P-element vector pWIZ [19] (link). Validation of the capaR RNAi line was confirmed by quantitative Q-RT-PCR using the primers 5′-GCTCTCCTTTGTGCGGGGGCACAT-3′ and 5′-GCACGTCAGAGCCAGCCAGCATCC-3′ (Fig. S1). To generate the capaR-GAL4 driver, the putative promotor sequence of the capaR gene was amplified by PCR using wild-type genomic DNA as a template with the primers 5′-CAGTCGACACCGGCAACCAC-3′and 5′-TTTAGCCCAGAGCTGAATGT-3′. The resulting amplicon (corresponding to bases −1 to −1501 from the transcriptional start site of the capaR coding region) was digested with KpnI and subcloned into pinGAL4 vector (gift of Dr. Jean-Christophe Billeter), which had previously digested with KpnI and CIP-treated. The ORF of the human neuromedin U receptor 2 (also referred to as FM4) was amplified from full-length cDNA clone (MHS1010-98075312, Thermo scientific) using specific primers: 5′-CACCATGTCAGGGATGGAAAAACTTC-3′ and 5′-TCAGGTTTTGTTAAAGTGGAAGCTTTG-3′. The ORF of the NMUR 2 gene was cloned into the pUAST vector using the Gateway system. The entry and destination vectors used were obtained from the Drosophila Gateway Vector collection (Invitrogen). All Transgenic lines were generated using standard methods for P-element-mediated germline transformation (BestGene Inc, USA).
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Publication 2012
Actins Animals, Transgenic apoaequorin Base Pairing Calcium Cells Cloning Vectors Cytosol Diet Diuretics DNA, Complementary DNA Fingerprinting Drosophila Episodic Ataxia, Type 2 Gene Expression Genes Genome Germ Line Homo sapiens Homozygote Humidity Introns Light Luminescence neuromedin U receptor Neuropeptides Oligonucleotide Primers Promoter, Genetic Reverse Transcriptase Polymerase Chain Reaction RNA Interference SERPINA3 protein, human Tail Tissues Tissue Specificity Transcription Initiation Site Urate Oxidase

Most recents protocols related to «Urate Oxidase»

Height, weight, body mass index (BMI), and waist circumference (WC) were measured with participants in the standing position. BMI was calculated by dividing body weight (kg) by height in meters squared (m2). SBP and diastolic BP (DBP) were measured at the upper arm in participants who had been seated for at least 5 min. BPs were measure once or twice. First measurements were used in the analysis. Serum levels of total cholesterol (mg/dL; TC: Ultra. Violet‐End [UV‐End] method using cholesterol dehydrogenase), high‐density‐lipoprotein cholesterol (mg/dL; HDL‐C: Direct method), and triglycerides (mg/dL; TGs: Enzymatic method) were also measured. LDL‐C was estimated using the Friedewald equation ([TC]—[HDL‐C]—[TGs/5]).16 SUA levels were also measured using an enzymatic method (Uricase‐POD). Hemoglobin A1c (HbA1c) levels were determined by latex agglutination turbidimetry. The estimated glomerular filtration rate (eGFR) was calculated using the Japanese GFR equation: eGFR (mL/min/1.73 m2) = 194 × Cr−1.094 × age−0.287 (×0.739 if female).17 Chronic kidney disease (CKD) was diagnosed as eGFR <60 mL/min/1.73 m2 based on the Japanese guideline.
Participants were asked to complete a self‐administered questionnaire that addressed healthy lifestyle characteristics (alcohol consumption, smoking behavior) and present medical history of comorbidities such as hypertension, diabetes mellitus, dyslipidemia, hyperuricemia, cardiovascular disease, cerebrovascular disease, and renal disease. Participants who answered that they had any of these comorbidities were registered as having a present medical history.
Publication 2023
Arm, Upper Body Weight Cardiovascular Diseases Cerebrovascular Disorders Cholesterol cholesterol dehydrogenase Chronic Kidney Diseases Diabetes Mellitus Dyslipidemias Enzymes Glomerular Filtration Rate Hemoglobin A, Glycosylated High Blood Pressures High Density Lipoprotein Cholesterol Hyperuricemia Index, Body Mass Japanese Kidney Diseases Latex Fixation Tests Pressure, Diastolic Serum Triglycerides Turbidimetry Urate Oxidase Viola Waist Circumference Woman
Serum uric acid (micromoles per liter) was measured by the enzymatic uricase method. Variation for uric acid determinations were <2.8% at 164 μmol/L (2.76 mg/dL), 2.3% at 470 μmol/L (7.90 mg/dL), and 1.8% at 624 μmol/L (10.49 mg/dL). Covariates included sex (men/women), age (years), blood glucose (millimoles per liter), total cholesterol (millimoles per liter), triglycerides (millimoles per liter), and estimated glomerular filtration rate (eGFR; milliliters per minute per 1.73 m2) at baseline.
Publication 2023
Blood Glucose Cholesterol EGFR protein, human Enzymes Glomerular Filtration Rate PER1 protein, human Serum Triglycerides Urate Oxidase Uric Acid Woman
Blood samples were treated with uricase, and the amount of H2O2 formed was measured at 510 nm by peroxidase-catalyzed reaction with 4-aminophenazone and chlorophenol, which produces a colored quinoneimine product [31 (link)]. The uric acid concentration was expressed as a milligram of urate per milliliter of blood (mg/mL).
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Publication 2023
Aminopyrine BLOOD Chlorophenols Peroxidase Peroxide, Hydrogen Urate Urate Oxidase Uric Acid
Blood samples were taken between 8:00 and 9:00 a.m. after overnight fasting. Fasting plasma glucose (FPG), hemoglobin A1c (HbA1c), insulin, lipid profile (total cholesterol, high-density lipoprotein (HDL) cholesterol, and triglycerides), uric acid, and liver markers were analyzed in serum. Using duplicate samples, the radioimmunoassay method (Behring, Scoppito, Italy) was applied to measure the serum insulin concentrations. A competitive luminometric method based on the solid-phase antigen luminescent technology (SPALT) principle was employed to assess the serum concentrations of TSH, FT3, and FT4 (LIAISON FT3, FT4, TSH, DiaSorin, Saluggia, Italy). Fasting plasma lipid concentrations (triglycerides, total cholesterol, and HDL cholesterol) were measured using an automated colorimetric method, and fasting plasma glucose concentrations were determined using the glucose oxidase method (Sclavus, Siena, Italy) (Hitachi; Boehringer Mannheim, Mannheim, Germany). An Architect c8000 chemical analyzer was used to measure glycated hemoglobin (HbA1c) (Abbott).
The URICASE/POD method was employed to quantify the amount of uric acid in the blood using an autoanalyzer (Boehringer Mannheim). Standard laboratory procedures were used to measure amino transferase, -glutamyl transpeptidase (GT), and creatinine with an automated system (UniCel Integrated Workstations DxC 660i, Beckman Coulter, Fullerton, CA, USA). The Friedewald equation [30 (link)] was used to calculate LDL cholesterol. DxI/Access was used to perform a quantitative analysis of serum ferritin using Access Ferritin Reagent Packs (Beckman-Coulter AB, Bromma, Sweden). Radioimmunoassay (Behring, Scoppito, Italy) was used to measure the levels of serum insulin, and chemiluminescence was applied to determine the levels of serum 25(OH) vitamin D (Diasorin Inc., Stillwater, OK, USA). Insulin resistance was calculated using the Homeostasis Model Assessment-Insulin Resistance (HOMA-IR) method: ((fasting insulin × fasting glucose)/405, normal range 0.23–2.5) [31 (link)].
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Publication 2023
Antigens BLOOD Chemiluminescence Cholesterol Cholesterol, beta-Lipoprotein Colorimetry Creatinine Ferritin gamma-Glutamyl Transpeptidase Glucose Hemoglobin, Glycosylated Hemoglobin A, Glycosylated High Density Lipoprotein Cholesterol Homeostasis Insulin Insulin Resistance Lipids Liver Luminescence Oxidase, Glucose Plasma Radioimmunoassay Serum Transferase Triglycerides Urate Oxidase Uric Acid Vitamin D
Uric acid is a body waste product formed due to breakdown of purines and one of the markers for assessing of Kidney functions. It is a regular eliminatory product from the body. The plasma levels of uric acid from normoxia, hypobaric hypoxia exposed and quercetin supplemented groups was estimated using commercially available uric acid kit provided by Synergy bio (Uricase method) as per manufacturer’s instructions.
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Publication 2023
Catabolism Human Body Hypoxia Kidney Plasma purine Quercetin Urate Oxidase Uric Acid

Top products related to «Urate Oxidase»

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Uricase is a laboratory equipment product manufactured by Merck Group. It is an enzyme that catalyzes the oxidation of uric acid to allantoin, a more soluble compound. Uricase is used in clinical and research settings to measure uric acid levels in biological samples.
Sourced in United States
The Amplex Red Uric Acid/Uricase Assay kit is a fluorometric assay designed to measure uric acid levels. It utilizes the Amplex Red reagent to detect the H2O2 produced by the uricase-catalyzed oxidation of uric acid.
Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, Canada, Belgium, Italy, Macao, India, Japan, Brazil, Poland
Uric acid is a laboratory reagent used in the quantitative determination of uric acid levels in biological samples, such as blood or urine. It is a chemical compound that serves as a diagnostic tool for various medical conditions, including gout, kidney disorders, and metabolic disorders. The core function of uric acid is to provide an analytical measurement of this substance in the body, which can help healthcare professionals assess and monitor a patient's health status.
Sourced in United States, Japan, Germany, United Kingdom, China, Italy, Canada
The AU5800 is a chemistry analyzer designed for high-throughput clinical laboratory testing. It features advanced optics and automation to provide reliable and efficient sample processing. The core function of the AU5800 is to perform a variety of clinical chemistry tests, including immunoassays, on patient samples.
Sourced in Germany
The URICASE/POD method is a laboratory technique used for the quantitative determination of uric acid levels in biological samples. It involves the enzymatic conversion of uric acid to allantoin, which is then detected and measured colorimetrically. This method provides a reliable and accurate way to assess uric acid concentrations in various clinical and research applications.
Sourced in United States, Germany, United Kingdom, Italy, France, Japan, Sao Tome and Principe
Allopurinol is a laboratory reagent used in the study of purine metabolism. It functions as an inhibitor of the enzyme xanthine oxidase, which is involved in the breakdown of purines. The core function of Allopurinol is to facilitate the investigation of purine-related metabolic processes in research settings.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
Sourced in Japan, Germany
The Hitachi Automatic Analyzer 7600-210 is a biochemical analysis instrument designed for clinical laboratories. It is capable of performing a range of biochemical tests, including measurements of various chemical compounds, enzymes, and other biomolecules in biological samples such as blood, urine, and other bodily fluids.

More about "Urate Oxidase"

Urate oxidase, also known as uricase, is a crucial enzyme involved in the metabolism of purines, a group of organic compounds that include uric acid.
This enzyme catalyzes the oxidation of uric acid, a byproduct of purine metabolism, into a more soluble compound called allantoin.
Allantoin can be more easily excreted from the body, making urate oxidase an important player in maintaining healthy uric acid levels.
Urate oxidase is found in a variety of organisms, including humans, where its deficiency can lead to hyperuricemia, a condition characterized by high levels of uric acid in the blood.
Hyperuricemia is associated with the development of gout, a type of arthritis caused by the accumulation of uric acid crystals in the joints.
The Amplex Red Uric Acid/Uricase Assay kit is a commonly used tool for measuring uric acid levels, as it utilizes the uricase enzyme to oxidize uric acid and produce a fluorescent signal that can be detected.
The AU5800 and URICASE/POD methods are also popular techniques for quantifying uric acid concentrations.
Allopurinol, a medication used to treat gout, works by inhibiting the activity of xanthine oxidase, an enzyme involved in the production of uric acid.
This in turn helps to lower uric acid levels and reduce the risk of gout attacks.
Bovine serum albumin (BSA) is often used as a stabilizing agent in various biochemical assays, including those involving urate oxidase, to help maintain the enzyme's activity and structural integrity.
The Hitachi Automatic Analyzer 7600-210 is a widely used instrument for the clinical analysis of various biomarkers, including uric acid, and may be employed in conjunction with urate oxidase-based methods for measuring uric acid levels.
Optimizing research protocols for urate oxidase is crucial for advancing our understanding of purine metabolism and developing effective therapies for conditions like gout.
The PubCompare.ai platform can help researchers identify the most effective and reproducible protocols, ensuring that their work contributes to the growing body of knowledge in this important field of study.