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Purification and properties of urate oxidase from Streptomyces cyanogenus.
J Biochem. 1981 Jun; 89(6):1769-76.JB

Abstract

Urate oxidase [EC 1.7.3.3] was purified to homogeneity from cell-free extracts of a strain of Streptomyces cyanogenus. The enzyme had a molecular weight of 100,000 and consisted of three subunits each with a molecular weight of 32,000. The isoelectric point was at pH 4.0. No evidence was found for the involvement of copper, iron or coenzymes in the urate oxidase reaction. The enzyme was most active at pH 8 and at 35 degrees C, and was stable between pH 6 and 11 (35 degrees C, 1 h) and below 50 degrees C (pH 7.8, 10 min). The enzyme was inhibited by cyanide and sulfhydryl reagents, but only slightly by heavy metal ions and chelating agents. The activity was inhibited by xanthine and 2-hydroxypurine. The enzyme was found not to be inhibited by high concentrations of uric acid when the activity was assayed in terms of hydrogen peroxide formation. Urea and racemic allantoin were formed from uric acid by the enzyme reaction in phosphate buffer, and urea and other ninhydrin-positive materials in borate buffer.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7287651

Citation

Ohe, T, and Y Watanabe. "Purification and Properties of Urate Oxidase From Streptomyces Cyanogenus." Journal of Biochemistry, vol. 89, no. 6, 1981, pp. 1769-76.
Ohe T, Watanabe Y. Purification and properties of urate oxidase from Streptomyces cyanogenus. J Biochem. 1981;89(6):1769-76.
Ohe, T., & Watanabe, Y. (1981). Purification and properties of urate oxidase from Streptomyces cyanogenus. Journal of Biochemistry, 89(6), 1769-76.
Ohe T, Watanabe Y. Purification and Properties of Urate Oxidase From Streptomyces Cyanogenus. J Biochem. 1981;89(6):1769-76. PubMed PMID: 7287651.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and properties of urate oxidase from Streptomyces cyanogenus. AU - Ohe,T, AU - Watanabe,Y, PY - 1981/6/1/pubmed PY - 1981/6/1/medline PY - 1981/6/1/entrez SP - 1769 EP - 76 JF - Journal of biochemistry JO - J Biochem VL - 89 IS - 6 N2 - Urate oxidase [EC 1.7.3.3] was purified to homogeneity from cell-free extracts of a strain of Streptomyces cyanogenus. The enzyme had a molecular weight of 100,000 and consisted of three subunits each with a molecular weight of 32,000. The isoelectric point was at pH 4.0. No evidence was found for the involvement of copper, iron or coenzymes in the urate oxidase reaction. The enzyme was most active at pH 8 and at 35 degrees C, and was stable between pH 6 and 11 (35 degrees C, 1 h) and below 50 degrees C (pH 7.8, 10 min). The enzyme was inhibited by cyanide and sulfhydryl reagents, but only slightly by heavy metal ions and chelating agents. The activity was inhibited by xanthine and 2-hydroxypurine. The enzyme was found not to be inhibited by high concentrations of uric acid when the activity was assayed in terms of hydrogen peroxide formation. Urea and racemic allantoin were formed from uric acid by the enzyme reaction in phosphate buffer, and urea and other ninhydrin-positive materials in borate buffer. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/7287651/Purification_and_properties_of_urate_oxidase_from_Streptomyces_cyanogenus_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/89.1769?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -