Isolatin and characterization of Peroxidase from Breast Cancer (Part II)
Rafidain Journal of Science,
2007, Volume 18, Issue 3, Pages 58-70
AbstractThe research was concerned with isolation and characterization of peroxidase from breast cancer tissues using different biochemical techniques. Two proteinous components had been isolated by gel filtration chromatography from the precipitate produced by ammonium sulphate saturation. It was found that only the second peak had peroxidase activity.
The apparent molecular weight of the isolated peroxidase using gel filtration chromatography and SDS–electrophoresis was determined and found to be (39800) Dalton.
Finally, the research specifies the optimum conditions for peroxidase activity. Maximum activity was obtained using (20) mM of guaiacol as a substrate for the enzyme, sodium phosphate (150 mM) as a buffer at pH (6) for (5) minutes at (40) °C. Using linweaver–burk plot, it was found that maximum velocity (Vmax) and Michaelis constant (km) had the values of (135.37) µmol/ min and (2.56) mM respectively. The effect of some chemical compounds and drugs on the peroxidase activity was also studied. It was found that manganase chloride (MnCl2) showed a competitive inhibition on the activity of the enzyme at a concentration of (10) mmol.
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