PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2004 | 53 | 1 |

Tytuł artykułu

Purification and characterization of extracellular Pseudomonas aeruginosa urate oxidase enzyme

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Urate oxidase (uricase) was isolated and purified from Pseudomonas aeruginosa to apparent homogeneity using ammonium sulphate precipitation followed by ion exchange and gel filtration chromatography. The specific activity of the purified uricase enzyme was found to be 636.36 with the use of uric acid as a substrate. The purified uricase enzyme is a monomeric protein with molecular weight of 64 kilodaltons. The optimal pH and temperature of the purified enzyme is 9.0 and 30°C, respectively. The effect of some metal ions was studied. Sulphate forms of Fe⁺², Zn⁺² and Co⁺² inhibit the uricolytic activity whereas; NaCl and CaCl₂ enhance the enzyme activity. Moreover, the purified enzyme is inhibited by EDTA and KCN.

Wydawca

-

Rocznik

Tom

53

Numer

1

Opis fizyczny

p.45-52,fig.,ref.

Twórcy

autor
  • University of Alexandria, Chatby 21526, Alexandria, Egypt
autor
autor

Bibliografia

  • Atsuo T., Y. Midori, K. Susumu and F. Saburo. 1977. Production of uricase by Candida tropicalis using n-alkane mixture as substrate. Appl. Environ. Microbiol. 34:342-346.
  • Bongaerts G.P.A. and G.D. Vogels. 1976. Uric acid degradation by Bacillus fastidiosus strains. J. Bacteriol. 125: 689-697.
  • Bongaerts G.P.A., I.L. Sin, A.L.J. Peters and G.D. Vogels. 1977. Purine degradation in Pseudomonas aeruginosa and Pseudomonas testosteroni. Biochim. Biophys. Acta 499: 111-118.
  • Bradford M.M. 1976. A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
  • Brenard K., X.W. Wu, C.C. Lee, D.M. Muzny and C.T. Caske. 1989.Urate oxidase: primary structure and evolutionary implications. Proc. Natl. Acad Sci. USA 86: 9412-9416.
  • Itaya K., J. Fukumoto and T. Yamaman. 1971. Studies on urate oxidase of Candida utilis. II. Some physical and chemical properties of the purified enzyme. Agric. Hist. Chem. 35: 813-821.
  • Kaltwasser H. 1971 .Studies on the physiology of Bacillus fastidiosus. J. Bacteriol. 107: 780-788.
  • Laemmli U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680.
  • Lee C.C, X. Wu, R.A. Giggs, R.G. Cook, D.M. Muzny and T. Caskey. 1988. Generation of cDNA probes directed by amino acids sequence: cloning of urate oxidase. Science 293: 1288-1291.
  • Liu J.G., G.X. Li, H. Liu and X.K. Zhou. 1994. Purification and properties of uricase from Candida sp. and its application in uric acid analysis in serum. Appl. Biochem. Biotech. 47: 1.
  • Massey V., H. Komai, G. Palmer and G.B. Elion. 1970. On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo [3,4 d] pyrimidines. J. Biol. Chem. 245: 2837-2844.
  • Mahler J.L. 1970. A new bacterial uricase for uric acid determination. Anal. Biochem. 38: 65-84.
  • Sambrook J., E.F. Fritsch and T. Maniatis. 1989. Molecular cloning. A laboratory Manual. Cold Spring Harbor Laboratory, NY.
  • Sanger F., S. Nicklen and A.R. Coulson. 1977. DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. USA 74: 5463-5467.
  • Van der Drift L. and G.D. Vogels. 1975. Allantoin racemase: a new enzyme from Pseudomonas species. Biochim. Biophys. Acta 391:240-248.
  • Wu X., M. Wakamiya, S. Vaishnav, R. Geske, C. Montgomery, P. Jones, A. Bradley and T. Caskey. 1994. Hyperuricemia and urate nephropathy in urate oxidase deficient mice. Proc. Natl. Acad. Sci. USA 91: 742-746.
  • Zhu X.J., J.G. Liu and G.X. Li. 2001. Cloning and expression of urate oxidase and its application in serum uric acid analysis. Chinese J. Biotechnol. 6: 68-72.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-69f7e949-4d52-4580-8476-30cc3b07b329
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.