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2 edition of expression of human urate oxidase. found in the catalog.

expression of human urate oxidase.

Laurence A. De-Netto

expression of human urate oxidase.

by Laurence A. De-Netto

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Published by University of Wolverhampton in Wolverhampton .
Written in English


Edition Notes

Dissertation Ph.D. - University of Wolverhampton, 1996.

ID Numbers
Open LibraryOL19785679M

Leach, M., et al., (), Efficacy of Urate Oxidase (Uri- cozyme) in Tumor Lysis Induced Urate Nephropathy, Clini- cal and Laboratory Haematology Legoux, R., et al., (), Cloning and Expression in Escherichia coli of the Gene Encoding Aspergillus flavus Urate Oxidase Journal of Biological Chemistry This article is from SpringerPlus, volume ctUrate oxidase is an important enzyme with therapeutic and diagnostic applications. Rasburicase is a.

  Ichida K, Hosoyamada M, Kimura H, Takeda M, Utsunomiya Y, Hosoya T, et al. Urate transport via human PAH transporter hOAT1 and its gene . urate oxidase proteins invention relates Prior art date Application number SGA Inventor Jacob Hartman Simona Mendelovitz Original Assignee Savient Pharmaceuticals Inc Priority date (The priority date is an assumption and is not a legal conclusion.

The human urate oxidase (E.C. ) gene, UOX, is assigned to chromosome 1 by Southern analysis of human × hamster cell hybrids. Using fluorescent in . Urate oxidase (Uox), a therapeutic enzyme for treatment of hyperuricemia, is a homotetramer with multiple surface lysines, limiting conventional approaches for albumination. Incorporation of p-azido-l-phenylalanine into two predetermined positions of Uox allowed site-specific linkage of dibenzocyclooctyne-derivatized human serum albumin (HSA.


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Expression of human urate oxidase by Laurence A. De-Netto Download PDF EPUB FB2

This study, therefore, aims to express genetically modified human urate oxidase in the methylotrophic yeast Pichia pastoris. Accordingly, the genetically modified human urate oxidase was successfully expressed intracellularly and extracellularly under the control of an alcohol oxidase promoter and was subjected to the enzyme activity assay.

Genetically, the loss of urate oxidase function in humans was caused by two nonsense mutations at codons 33 and and an aberrant splice site. It has been proposed that the loss of urate oxidase gene expression has been advantageous to hominids, since uric acid is a powerful antioxidant and scavenger of singlet oxygen and s: UOX, UOXP, URICASE, Urate oxidase, urate.

In most mammals, the activity of urate oxidase catalyzes the oxidation of uric acid to allantoin; humans and some primates lack this enzyme loss of urate oxidase in the human during primate evolution predisposes man to hyperuricemia, a metabolic disturbance that can lead to gouty arthritis and renal stones (summary by Wu et al., ).

Urate oxidase is a key enzyme in purine metabolism and catalyzes the oxidation of uric acid to allantoin. expression of human urate oxidase. book It is used to treat hyperuricemia and gout, and also in a diagnostic kit.

In this study, error-prone polymerase chain reaction and staggered extension process was used to generate a mutant urate oxidase with improved enzyme activity from Bacillus subtilis. After several rounds of Cited by: 6.

Human urate oxidase gene: cloning and partial sequence analysis reveal a stop codon within the fifth exon.

Yeldandi AV, et al. Biochem Biophys Res Commun, Sep PMID ; Two independent mutational events in the loss of urate oxidase during hominoid evolution. Wu XW, et al. J Mol Evol, Jan.

PMID Exhibits urate oxidase activity. Involved in protein homotetramerization and urate catabolic process. Predicted to localize to peroxisome. Is expressed in liver and periderm.

Orthologous to human UOX (urate oxidase (pseudogene)). Genome Resources. flavus urate oxidase cDNA with an artificial promoter developed from gal7 (galactokinase) and adh2 (alcohol dehydrogenase II) promoters (it is repressed by glucose and induced by galactose) and with gal7 transcription termination sequence.

Some codons in the cDNA have been changed empirically in order to increase the stability of the mRNA. URAT1 (urate transporter 1) Aliases: OAT4L, RST Gene name: Solute carrier family 22 member 12 (SLC22A12) Summary. URAT1, a member of the OAT (organic anion transporter) family, is an anion-exchanging uptake transporter localized to the apical (brush border) membrane of renal proximal tubular cells [1, 2], where it mediates the re-absorption of uric acid from the proximal tubule, thereby.

Small-scale expression and time course study of urate oxidase expression in E. coli. Comassie Blue stained 12% SDS-PAGE (a) and respective Western blotting analysis (b) of urate oxidase induction in E.

coli. Lane M, protein BenchMarker (Invitrogen); Lane 1, supernatant of uninduced cells; Lanes 2–6, supernatant of induced cells af RESEARCH Open Access Cloning and expression of Aspergillus flavus urate oxidase in Pichia pastoris Ramin Fazel1, Najmeh Zarei2, Nasser Ghaemi1, Mohammad Mehdi Namvaran3, Somayeh Enayati2, Esmat Mirabzadeh Ardakani2, Mohammad Azizi2 and Vahid Khalaj2* Abstract Urate oxidase is an important enzyme with therapeutic and diagnostic applications.

Urate oxidase (EC ) plays an important role in purine degradation pathway and catalyzes uric acid oxidation into allantoin, H 2 O 2 and CO 2 in the presence of oxygen (Collings et al. ).The Aspergillus flavus urate oxidase ( kDa) contains four identical subunits, in which each subunit is associated with one active site.

Urate oxidase is a non-glycosylated enzyme having no intra. J Wu XW, et al., Urate oxidase: primary structure and evolutionary implications. Proc Natl Acad Sci U S A. Dec;86(23) Proc. In order to study the bovine urate oxidase (urate oxidase; EC ) expression in prokaryotic system, we constructed pETUO expression vector and optimized the its expression condition.

We determined the urate oxidase activity of its expression. The results showed that the bovine urate oxidase that we expressed was about 34 ku. In the optimum temperature of 42°C, the determination.

gout and preventing tumor lysis syndrome in human patients. hyperuricemia | pseudogene | evolution U ric acid (monosodium urate) is a metabolic product of pu-rine catabolism generated from the breakdown of nucleic acids. In most species, uric acid is metabolized to 5-hydroxyisourate by the enzyme uricase (urate oxidase) (1).

Depending on the. Proc. Natl. Acad. Sci. USA86 () UO mouse SOD yeast SOD human SOD bovine Cp human CCO bovine CCO human [K N G I KH V H A F I H T P T T H F C E V E40 N A E R GFHI H E F G D A T D VRAG P Hf 40 G L H FHVHQ F G N D T A T S A G P H 40 G D H G F V 8 Q F G D N T Q G T S A G P 87 L H T V F H G H S F Q Y K H R JVYLS S D V F 18 E L LHFH D H T L M I V F L I S S L V L Y I 18.

The normal reference range for urate in human blood is to mg/dL in women and – mg/dL in men. When the level of urate is > mg/dL ( μmol/l), the limit of solubility under physiological conditions, crystals of urate may form as monosodium urate (MSU).

Accordingly, the genetically modified human urate oxidase was successfully expressed intracellularly and extracellularly under the control of an alcohol oxidase promoter and was subjected to the. K e y w o r d s: Urate oxidase (uricase), P. aeruginosa, C. flavigena, partial coding sequence Introduction Urate oxidase or uricase (urate oxygen oxidoreductase, EC ) is an enzyme that catalyzes the oxidation of uric acid to unidentified product then to a more soluble compound, allantoin.

Uricase occupies. George Nuki, in Gout & Other Crystal Arthropathies, Introduction. Uricase or urate oxidase (EC ) is a copper-binding enzyme that catalyses the oxidation of uric acid to 5-hydroxyisourate and hydrogen peroxide (H 2 O 2) (Fig.

).Subsequent hydrolysis and decarboxylation leads to the formation of allantoin as the end product of purine metabolism in most prokaryotic and eukaryotic.

The expression of human urate oxidase. (Thesis) De-Netto LA. Publisher: University of Wolverhampton [] Metadata Source: The British Library Type: Thesis.

Abstract. Highlight Terms No biological terms identified No abstract supplied. Menu Formats. Abstract; Thesis at EThOS.

Cloning and expression of a urate oxidase and creatinine hydrolase fusion gene in Escherichia coli. [Xin Cheng, Fang Liu, Yanxin Zhang, Yunsheng Jiang] PMID Abstract To construct a plasmid containing a urate oxidase and creatinine hydrolase fusion gene and transform the plasmid into Escherichia coli to decompose uric acid and.

Background. Urate oxidase (EC ) plays an important role in purine degradation pathway and catalyzes uric acid oxidation into allantoin, H 2 O 2 and CO 2 in the presence of oxygen (Collings et al. ).The Aspergillus flavus urate oxidase ( kDa) contains four identical subunits, in which each subunit is associated with one active site.

Urate oxidase is a non-glycosylated enzyme.ting the expression of urate oxidase is limited in verte-brates, except for the activation of rat urate oxidase after treatment with glucagon or carbon tetrachloride (CCl 4) [10,11], and the identification of regulatory ele-ments in the urate oxidase promoter of hominoids [6].