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Differential pH sensitivity of tissue superoxide dismutases
Samir P Patel1, Surendra S Katyare
1Department of Biochemistry, Faculty of Science, The Maharaja Sayajirao University of Baroda, 390 002 Vadodara, Gujarat India.
Indian Journal of Clinical Biochemistry : IJCB
|October 30, 2012
Summary
Superoxide dismutase (SOD) activity varies between human and rat tissues and cellular fractions. Optimal SOD measurement for accurate results is recommended at pH 8.0, not pH 9.2.
Area of Science:
- Biochemistry
- Enzymology
- Cellular Biology
Background:
- Superoxide dismutase (SOD) is a critical antioxidant enzyme.
- SOD activity is vital for cellular protection against oxidative stress.
- Understanding SOD activity across different tissues and cellular compartments is important.
Purpose of the Study:
- To determine superoxide dismutase (SOD) activities in various human and rat biological samples.
- To assess the pH stability of SOD enzymes from different sources.
- To identify optimal conditions for measuring SOD activity.
Main Methods:
- Superoxide dismutase (SOD) activity was measured using the pyrogallol assay.
- Assays were performed on human and rat red blood cells (RBCs), and rat liver, kidney, brain, and heart mitochondria and cytosolic fractions.
- Measurements were conducted in potassium phosphate buffer at pH 8.0 and 9.2.
Main Results:
- SOD enzymes exhibited differential pH stability, with varying susceptibility at pH 9.2.
- Mitochondrial and cytosolic SOD content showed tissue-specific patterns within the same organ.
- SOD activity measurements at pH 8.0 appeared to provide more realistic estimates.
Conclusions:
- SOD activity is not uniform across different tissues and cellular compartments.
- The pH stability of SOD varies, impacting measurement accuracy.
- pH 8.0 is suggested as a more reliable condition for SOD activity determination.
