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Acta Physiologica Hungarica
Authors: A Todorović, A Todorović, A Todorović, S Pejić, S Pejić, S Pejić, J Kasapović, J Kasapović, J Kasapović, V Stojiljković, V Stojiljković, V Stojiljković, SB Pajović, SB Pajović, SB Pajović, DT Kanazir, DT Kanazir, and DT Kanazir

In order to examine if differences in activity and inducibility of antioxidative enzymes in rat cerebral cortex and hippocampus are underlying their different sensitivity to radiation, we exposed four-day-old female Wistar rats to cranial radiation of 3 Gy of g-rays. After isolation of hippocampus and cortex 1 h or 24 h following exposure, activities of copper-zinc superoxide dismutase (CuZnSOD), manganese superoxide dismutase (MnSOD) and catalase (CAT) were measured and compared to unirradiated controls. MnSOD protein levels were determined by SDS-PAGE electrophoresis and Western blot analysis. Our results showed that CuZnSOD activity in hippocampus and cortex was significantly decreased 1 h and 24 h after irradiation with 3 Gy of g-rays. MnSOD activity in both brain regions was also decreased 1 h after irradiation. 24 h following exposure, manganese SOD activity in hippocampus almost achieved control values, while in cortex it significantly exceeded the activity of the relevant controls. CAT activity in hippocampus and cortex remained stable 1 h, as well as 24 h after irradiation with 3 Gy of g-rays. MnSOD protein level in hippocampus and cortex decreased 1 h after irradiation with 3 Gy of g-rays. 24 h after exposure, MnSOD protein level in cortex was similar to control values, while in hippocampus it was still significantly decreased. We have concluded that regional differences in MnSOD radioinducibility are regulated at the level of protein synthesis, and that they represent one of the main reasons for region-specific radiosensitivity of the brain.

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Acta Alimentaria
Authors: D. Filipović, J. Kasapović, S. Pejić, A. Nićiforović, S. B. Pajović, and M. B. Radojčić

Specific composition, protein profiles and total SOD activity were analysed in full milk samples obtained from five farms of the Milk Company IMPAZ. The effects of several laboratory treatments on milk proteins SDS-PAGE profiles and the respective SOD activity were also followed. The total SOD activity was detected in all full milk samples, and its values varied between 2 and 3 U mg-1 protein. The enzyme could be partially purified, up to »5 U mg-1 protein, by ethanol extraction. The recovered SOD activity in ethanol extract was proportional to the initial full milk SOD activity. The disruption of casein micelles by Ca2+ removal was followed by a significant decrease in SOD activity to 1.24-0.18 U mg-1 protein. The loss of enzyme activity was ascribed to the changes in milk milieu induced by dissociation of casein micelles.

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