scholarly journals XANTHINE OXIDASE ACTIVITY IN REGENERATING LIVER

1957 ◽  
Vol 41 (2) ◽  
pp. 233-242 ◽  
Author(s):  
Muriel Feigelson ◽  
Philip Feigelson ◽  
Paul R. Gross
Keyword(s):  
Enzyme Activity ◽  
Xanthine Oxidase ◽  
Adrenal Cortex ◽  
Oxidase Activity ◽  
Minor Role ◽  
Regenerating Liver ◽  
Liver Growth ◽  
Tissue Weight ◽  
Xanthine Oxidase Activity ◽  
A Minor

The xanthine oxidase activity of mouse regenerating liver has been shown to be elevated during the period of rapid liver growth and proliferation. This increase is evident when the enzyme activity is expressed per unit wet tissue weight, per unit nitrogen, or per cell. The adrenal cortex probably plays only a minor role in implementing this phenomenon. Further augmentation of the xanthine oxidase level of regenerating liver is not induced by the administration of large quantities of the substrate, xanthine, to the animal.

Activity and stability of rat liver xanthine oxidase in the presence of pyridine

2011 ◽  
Vol 89 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Kaveh Amini ◽  
Mohammad-Hossein Sorouraddin ◽  
Mohammad-Reza Rashidi
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Xanthine Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Enzyme Inactivation ◽  
Native Enzyme ◽  
Buffer Solution ◽  
Stability Parameters ◽  
Xanthine Oxidase Activity

In the present study, rat liver xanthine oxidase activity and its thermostability in the presence of pyridine were investigated. The activity of the enzyme was determined by following the formation of uric acid spectrophotometrically. The thermal stability of the enzyme was studied in the presence of 0.0%–2.0% of pyridine in Sorenson’s buffer. Thermal stability parameters (half-life, inactivation constant, and activation energies for enzyme inactivation), thermodynamic constants (ΔH*, ΔS*, and ΔG*) and the kinetic parameters (Km and Vmax), were determined in pyridine-free and pyridine-containing buffer solution. A dramatic reduction was observed in xanthine oxidase activity in the presence of pyridine. However, the pyridine-treated enzyme showed a marked enhancement in thermal stability compared with the native enzyme. The ΔG values for the enzyme activity in the presence of pyridine were found to be about 1.5-fold larger than that calculated for the native enzyme, indicating that the enzyme becomes kinetically more stable in the presence of pyridine. The Km value for xanthine oxidase in the presence of 0.5% pyridine increased by 4.8-fold compared with the enzyme in the pyridine-free buffer solution; however, there was 1.8-fold reduction in the Vmax value in the hydro-organic solution compared with the enzyme activity in the buffer solution. As the stability of enzymes is one of the most difficult problems in protein chemistry, this thermostability property of xanthine oxidase could be of great value in developing novel strategies to improve and expand its application in various areas.

Stabilization of Xanthine Oxidase Activity by Salicylate

Nature ◽  
1956 ◽  
Vol 178 (4524) ◽  
pp. 88-89 ◽  
Author(s):  
F. BERGEL ◽  
R. C. BRAY
Keyword(s):  
Xanthine Oxidase ◽  
Oxidase Activity ◽  
Xanthine Oxidase Activity

Effect of acetyl-l-carnitine on lipid peroxidation and xanthine oxidase activity in rat skeletal muscle

1993 ◽  
Vol 18 (11) ◽  
pp. 1157-1162 ◽  
Author(s):  
C. Di Giacomo ◽  
F. Latteri ◽  
C. Fichera ◽  
V. Sorrenti ◽  
A. Campisi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Lipid Peroxidation ◽  
Xanthine Oxidase ◽  
Oxidase Activity ◽  
Rat Skeletal Muscle ◽  
Xanthine Oxidase Activity
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