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Öğe Influence of lycopene and cysteamine on sperm and oxidative stress parameters during liquid storage of ram semen at 5°C(Elsevier Science Bv, 2016) Peker Akalin, Pinar; Bucak, Mustafa Numan; Gungor, Sukru; Baspinar, Nuri; Coyan, Kenan; Dursun, Sukru; Ili, PinarEjaculates were collected from six Merino rams with the aid of an artificial vagina twice a week. The ejaculates containing spermatozoa with >80% forward progressive motility and concentrations higher than 2 x 10(6) spermatozoa/ml were pooled. The present study included two experiments. In experiment 1, each pooled ejaculate was divided into four equal aliquots and diluted (37 degrees C) with the Tris based extender, containing 0 (control), 0.5, 1 and 2 mM lycopene, at a final concentration of approximately 400 x 10(6) sperms/ml (single step dilution), In experiment 2, cysteamine at concentrations of 0 (control), 0.5,1 and 2 mM, was used as an additive in the extender, and the procedure explained above was applied for the division of aliquots and the dilution of semen. Diluted semen samples were kept in glass tubes and cooled from 37 degrees to 5 degrees C in a cold cabinet, and maintained at 5 degrees C. Sperm and oxidative stress parameters were evaluated after 0, 24, 48 and 72 h of storage at 5 degrees C. The extender supplemented with 0.5 mM lycopene resulted in higher mitochondrial activity rate (p<0.05) in comparison to the control group at 72 h of storage. Lycopene at 0.5 mM dose led to higher sperm motility rate (p<0.05) when compared to 2 mM lycopene group at 72 h of liquid storage. As regards oxidative stress parameters, only 2 mM lycopene increased total glutathione levels (p<0.05) at 0 h of storage. The extender supplemented with 1 mM cysteamine gave higher motility (p<0.05) at 48 h compared to control. As regards oxidative stress parameters, 1 and 2 mM cysteamine at 48 h and 1 mM cysteamine at 72 h increased total glutathione levels (p<0.05) compared to control groups. Cysteamine at 1 and 2 mM doses decreased lipid peroxidation (p<0.05) at 0 h of liquid storage compared to control. Our data suggest that lycopene at 0.5 and 2 mM and cysteamine at 1 and 2 mM doses can be added to Tris based extender for improving the ram sperm motility, viability, mitochondrial activity and oxidative stress parameters during the liquid storage. (C) 2016 Elsevier B.V. All rights reserved.Öğe Melatonin Levels After Heat Treatment in Goat Milk: Relation of Total Protein(Kahramanmaras Sutcu Imam Univ Rektorlugu, 2022) Ispir, Medine; Peker Akalin, Pinar; Kazak, Filiz; Baspinar, NuriObjective of this study was to investigate the effects of pasteurization (15 seconds at 72 degrees C) and boiling processes (5 minutes at 100 degrees C) on goat milk melatonin and total protein levels. The milk of 20 healthy goats obtained from a private goat farm were used as materials. Each milk sample was divided into 3 for raw milk. for pasteurization and for boiling process. Melatonin levels in raw. pasteurized and boiled milk were determined with commercial ELISA kit. while total protein levels were determined spectrophotometricly by manual methods. Melatonin levels in boiled milk samples (4.20 +/- 0.39 pg ml(-1)) increased (P<0.05) compared to raw milk (3.19 +/- 0.25 pg ml(-1)) samples. While there was no difference between the heat-treated groups in terms of total protein levels determined by Bradford method. the total protein levels determined by Lowry method decreased significantly in boiling process group compared to the other groups (P<0.001). Positive correlations were determined between total protein levels determined by Bradford and Lowry methods in raw (r=0.723, P<0.01.), pasteurized (r=0.838, P<0.01) and boiled (r=0.149, P<0.05) milk samples. Pasteurization process applied to goat- milk did not change milk melatonin and total protein levels, and boiling process decreased total protein levels, while increased melatonin levels. Before melatonin analysis was performed in milk by ELISA method, it was predicted that a pre-treatment of milk may be useful in order to separate melatonin from the bound protein.