Nomenclature
CAS number: 9002-12-4
Urate oxidase; uric oxidase; urico-oxidase; uriKoxidase.
Description and references
An enzyme responsible for the oxidative scission
of the purine skeleton, and therefore of key importance to the catabolism
of nitrogenous compds in general in organisms that do not eliminate
intact uric acid or some other purine. All mammals except the primates
(including man) are uricolytic organisms. Porcine liver or bovine
kidney is the starting material for various purified prepns of uricase.
Isoln from porcine liver: Holmberg, Biochem.
J. 33, 1901 (1939); Miller et al., J. Biol. Chem. 216, 625 (1955); Robbins, Grant, US 2878161 (1959 to Armour). Review: Mahler, “Uricase” in The Enzymes vol. 8, P. D. Boyer et al., Eds. (Academic
Press, New York, 1963) pp 285-296.
Properties
Pale, brownish-green crystals or shiny, transparent,
striated plates. Practically insol in water. Slightly sol in buffered
alkali solns. Solns at pH 7.5-10.5 are relatively stable. Shows
unusually high absorption in the region of 330-350 nm (for highly
purified uricase: A1%276 = 11.3, A1%330 = 2.0, both in 1% Na2CO3; A280/A330 = 5.6). Isoelec. pt. pH 6.3. Copper content
of the enzyme (specific activity 120-125) equals ≈0.56 mg/g of enzyme
protein. There appears to be a satisfactory correlation between copper
content and activity of the purified enzyme. The enzyme is sensitive
to cyanide ion; the presence of 104M KCN inhibits
its activity.Use
In the determination of serum and urine uric acid.