Electron paramagnetic resonance of [(CH3) 4 N] 2 MnCl 4 and [(CH 3 ) 4 N] 2 FeCl 4 single crystals was studied between 20 and 400 K. The peak-to-peak derivative linewidths of these crystals seem not to change in this temperature interval and approximately 100 mT for [(CH 3 ) 4 N] 2 MnCl 4 and -20 mT for [(CH 3 ) 4 N] 2 FeCl 4 . The spectra were found to be isotropic, with g = 2.0039 for [(CH 3 ) 4 N] 2 MnCl 4 and g = 2.0042 for [(CH 3 ) 4 N] 2 FeCl 4 . This temperature independence is attributed to isotropic strong exchange interactions of Mn 2+ and Fe 2+ nuclei, and it seems that hindered rotation of the MnCl 4 " and FeCl 4 " tetrahedra does not occur in this temperature interval.
Catalase, one of the antioxidant enzymes, decomposes hydrogen peroxide into water and oxygen. From the discovery of catalase, several studies have been carried out to reveal its importance in health, food and cosmetics industries etc., and these studies are still ongoing. In this study, catalase enzyme was partially purified from muscle tissue of Dusky spinefoot (Siganus luridus). Purification procedure consisted of homogenate preparation, ammonium sulfate precipitation and dialysis. The enzyme was precipitated in the range of 40-60 % Ammonium Sulphate concentration. The optimum buffer was determined as 200 mM phosphate buffer, optimum pH 8.0 and optimum substrate concentration 24mM for H₂O₂, respectively.
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