An evolutionary loss of uricase in humans and higher primates has made this condition so common.

Drugs that may contribute to hyperuricosuria include allopurinol and uricase.

A man made uricase enzyme (rasburicase) is also available.

Most mammals possess the enzyme uricase, the doctors explained.

Alkalization is also not required if uricase is used.

Still, every mammal that lacks uricase is not equally susceptible to developing gout.

Gout is rare in most other animals due to their ability to produce uricase, which breaks down uric acid.

Uricase is required to breakdown uric acid.

In most other mammals, the enzyme uricase further oxidizes uric acid to allantoin.

The only possible solution to this problem must then be crossing Dalmatians with other breeds to reintroduce the "normal" uricase gene.

But sometime during the Miocene Epoch, mutations occurred in the gene that dictates the production of uricase.

Serum uric acid-lowering therapies: Where are we heading in management of hyperuricemia and the potential role of uricase.

Pegloticase is a recombinant porcine-like uricase.

A recombinant uricase enzyme (rasburicase) is available; its use, however, is limited, as it triggers an autoimmune response.

Pegloticase is a pegylated variant of the uricase enzyme which has been approved for the treatment of refractory gout.

In Dalmatian dogs, a lack of uricase (a genetic trait fixed in this breed) contributes to hyperuricemia and corresponding hyperuricosuria.

Uric acid is excreted by birds, reptiles, and some mammals that do not have a functional uricase gene, whereas other mammals produce allantoin.

Pegloticase (Krystexxa) - PEGylated uricase for the treatment of gout (Savient, 2010)

This led to the foundation of the Dalmatian-Pointer Backcross Project, which aims to reintroduce the normal uricase gene into the Dalmatian breed.

Hyperuricemia in Dalmatians (as in all breeds) is inherited, but unlike other breeds, the "normal" gene for uricase is not present in the breed's gene pool.

The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate:

In contrast to rasburicase, pegloticase is pegylated to increase its elimination half-life from about eight hours to ten or twelve days, and to decrease the immunogenicity of the foreign uricase protein.

The loss of uricase in higher primates parallels the similar loss of the ability to synthesize ascorbic acid, leading to the suggestion that urate may partially substitute for ascorbate in such species.

In legumes, 2 forms of uricase are found: in the roots, the tetrameric form; and, in the uninfected cells of root nodules, a monomeric form, which plays an important role in nitrogen-fixation.

Urate oxidase is known to be present in many mammals but does not naturally occur in humans.

Urate oxidase, a second marker for microbodies, was not detected in cell extracts.

It is the product of the oxidation of uric acid by urate oxidase.

Activities of urate oxidase and arylsulfatase-A did not change significantly but arylsulfatase-B was slightly decreased.

It is a recombinant version of urate oxidase, an enzyme that metabolizes uric acid to allantoin.

An evolutionary loss of urate oxidase (uricase), which breaks down uric acid, in humans and higher primates has made this condition common.

After confirmation of lysosome, de Duve's team was troubled by the existence of another enzyme urate oxidase in rat liver cell fraction.

Step one is catalysed by urate oxidase and step two is catalysed by hydroxyisourate hydrolase.

Patients at risk for acute uric acid nephropathy can be given allopurinol or rasburicase (a recombinant urate oxidase) prior to treatment with cytotoxic drugs.

Others include drugs that reduce the production of uric acid: xanthine oxidase inhibitors, urate oxidase (rasburicase), and sevelamer.

Biochemical Characterization of the HpxO Enzyme from Klebsiella pneumoniae, a Novel FAD-Dependent Urate Oxidase.

A recombinant urate oxidase enzyme, Elitek is the first recombinant uricolytic agent approved in the U.S. to maintain PUA levels in patients receiving anti-cancer therapy.

A procedure for cloning genes from genomic DNA using weakly hybridizing heterologous probes and a polymerase chain reaction-based screening: Cloning of the chickpea urate oxidase gene.

Allopurinol was also commonly used to treat tumor lysis syndrome in chemotherapeutic treatments, as these regimens can rapidly produce severe acute hyperuricemia, although it has gradually been replaced by urate oxidase therapy.

Rasburicase administration can cause anaphylaxis (incidence unknown); methemoglobinemia may occur in susceptible individuals such as those with G6PDH deficiency due to the production of hydrogen peroxide in the urate oxidase reaction.

In almost all land animals, urate oxidase further catalyzes the oxidation of uric acid to allantoin, but in humans and most higher primates, the urate oxidase gene is nonfunctional, so that UA is not further broken down.

Also called Elitek and recombinant urate oxidase.

Recombinant urate oxidase is a type of recombinant enzyme and a type of urate-lowering drug.

An evolutionary loss of uricase in humans and higher primates has made this condition so common.

A man made uricase enzyme (rasburicase) is also available.

Alkalization is also not required if uricase is used.

Most mammals possess the enzyme uricase, the doctors explained.

Other animals with uricase include fish, amphibians, and most non primate mammals.

Still, every mammal that lacks uricase is not equally susceptible to developing gout.

Gout is rare in most other animals due to their ability to produce uricase, which breaks down uric acid.

Drugs that may contribute to the cure or amelioration of hyperuricosuria include allopurinol and uricase.

Uricase is required to breakdown uric acid.

The absence of uricase in man may account for the high susceptibility of the human to acute renal failure.

In most other mammals, the enzyme uricase further oxidizes uric acid to allantoin.

The only possible solution to this problem must then be crossing Dalmatians with other breeds to reintroduce the "normal" uricase gene.

The regulation of intracellular urease and uricase activities was examined in Rhizopus oryzae.

Pegloticase is a recombinant porcine-like uricase.

Most mammals have a gene that makes an enzyme called uricase that breaks down uric acid, but humans lack the ability.

But sometime during the Miocene Epoch, mutations occurred in the gene that dictates the production of uricase.

Control of the R. oryzae uricase differs from that found in N. crassa and A. nidulans.

A recombinant uricase enzyme (rasburicase) is available; its use, however, is limited, as it triggers an autoimmune response.

Rhizopus oryzae, uricase, urease, nitrogen metabolism.

Pegloticase is a pegylated variant of the uricase enzyme which has been approved for the treatment of refractory gout.

In Dalmatian dogs, a lack of uricase (a genetic trait fixed in this breed) contributes to hyperuricemia and corresponding hyperuricosuria.

Uricase activity was estimated to be 0.6 mU g(-1) wet tissue in the liver and there appeared to be none in plasma and kidney.

Uric acid is excreted by birds, reptiles, and some mammals that do not have a functional uricase gene, whereas other mammals produce allantoin.

Rasburicase (Uricase) is an alternative to allopurinol and is reserved for patients who are high-risk in developing TLS.

Following uricase inhibition and shock the animals developed uric acid nephropathy, which was well discernible macroscopically and also proved by polarization microscopy.