Abstract
Optimum conditions for arginase in kidney tissue may differ from those for arginase of liver. Because optimum conditions for measuring arginase activity in rabbit kidney tissue were not determined, it was aimed to optimize arginase of rabbit kidney tissue and compare it with arginase of liver. In the present study, the kidneys of six New Zealand rabbits aged 1 year old were used. It was found to be preincubation temperature 53 °C, preincubation period is 15 minutes, incubation period is 10 minutes and optimum pH is 10.1 in NaHCO3-NaOH buffer for arginase in rabbit kidney tissue. Enzyme achieved its highest activity at 1 mM MnCl2concentration. Km of arginase in rabbit kidney tissue for L-arginine was measured as 12.5 mM. It was determined that Mn+2 ions and preincubation at 53 °C were essential for the activation of the enzyme. As a result, optimal conditions for the kidney arginase were found to be different from those for the liver arginase. Our study indicates that arginases encoded by separate gene loci may have different optimal conditions
Keywords
References
- Aminlari M, Shahbazkia HR, Esfandiari A (2007): Distribution of arginase in tissues of cat (Felis catus). J Feline Med Surg, 9 (2), 133-139.
- Benzer F, Temizer Ozan PS (2002): The levels of arginase enzyme activity in sheep with fasciolasis and some biochemical properties of arginase in liver tissue. FÜ Sağ Bil Vet Derg, 16 (2), 217-222.
- Colombo JP, Konarska L (1984): Arginase. In: Bergmayer GM. (Editor). Methods of Enzymatic Analysis. 3rd Edition, Weinheim: Vertag Chemie, 285-294.
- Dabir S, Dabir P, Somvanshi B (2005): Purification, properties and alternate substrate specificities of arginase from two different sources: Vigna catjang cotyledon and buffalo liver. Int J Biol Sci, 1 (3), 114-122.
- Dabir S, Dabir P, Somvanshi B (2006): The kinetics of inhibition of Vigna catjang cotyledon and buffalo liver arginase by L-proline and branched-chain amino acids. J Enzyme Inhib Med Chem, 21 (6), 727-731.
- Demir F, Ozan G, Temizer Ozan PS (2015): Ratlara uygulanan kurşun asetatın karaciğer arginazına etkisi ve enzimin bazı kinetik özellikleri. FÜ Sağ Bil Vet Derg, 29 (1), 37-43.
- Erdem N, Erişir M (2013): Tavşan Karaciğer Arginazının Optimize Edilmesi ve Dokulardaki Dağılımı. FÜ Sağ Bil Vet Derg, 27 (2), 81-86.
- Erişir M, Aydilek N, Aksakal M (2005): Effect of Vitamin E on Arginase Activity in the Liver and Kidneys of Testesterone Treated and Castrated Rabbits. Acta Vet Brno, 74, 527-531.
- Erişir M, Beytut E, Ozan TS, et al. (2003): Effects of dietary vitamin E and Selenium on Arginase Activity in the liver, kidney and heart of rats treated with high doses of glucocorticoids. Cell Biochem Funct, 21, 331-335.
- Erişir M, Erçel E, Yılmaz S, et al. (2005): Evaluation of optimal conditions for arginase activity in streptozotocin induced diabetic rats. Vet Med-Czech, 50, 69-76.
- Erişir M, Nazıroğlu M, Taşdemir B, et al. (2006): Effect of a dietary combined vitamin C and E supplementation on the liver, kidneys and brain arginase activity in non- pregnant and pregnant rats with streptozotocin-induced diabetes. Revue Med Vet, 157, 445-449.
- Erişir M, Tamser M, Taşdemir, et al. (2006): Ovariektomili Ratlara Estradiol 17-β ve Vitamin E Verilmesinin Arginaz Aktivitesi Üzerine Etkisi. Kafkas Üniv Vet Fak Derg, 12 (1), 31-35.
- Geyer JW, Dabich D (1971): Rapid method for determination of arginase activity in tissue homogenates. Anal Biochem, 39, 412-417.
- Glass RD, Knox WE (1973): Arginase isozymes of rat mammary gland, liver, and other tissues. J Biol Chem, 248, 5785-5789.
- Gotoh T, Sonoki T, Nagasaki A, et al. (1996): Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line. FEBS Lett, 395, 119-122.
- Guoyao WU, Morris SM (1998): Arginine metabolism: nitric oxide and beyond. Biochem J, 336, 1-17.
- Halifeoğlu İ (1993): İnsan Karaciğerinde, Eritrosit Ve Uterus Doku Arginazının Kinetik Özellikleri. Doktora Tezi, Elazığ Fırat Üniversitesi Tıp Fakültesi. Biyokimya Anabilim Dalı.
- Kadowaki H, Nesheim MC (1978): An assay for arginase in chicken kidney. Comp Biochem Physiol B, 61, 281–285.
- Kaysen GA, Strecker HJ (1973): Purification and properties of arginase of rat kidney. Biochem J, 133, 779- 788.
- Lowry OH, Rosenbrough NJ, Farr AL, et al. (1951): Protein measurements with the folin phenol reagent. J Biol Chem, 193, 265-275.
- Miyanaka K, Gotoh T, Nagasaki A, et al. (1998): Immunohistochemical localization of arginase II and other enzymes of arginine metabolism in rat kidney and liver. Histochem J, 30, 741–751.
- Powers GS, Meister T (1982): Urea synthesis and ammonia metabolism. In: Arias I, Popper H, Schachter D, Shafrits DA, editors: The liver: Biology and Pathobiology. Raven Press. New York, 251-263.
- Reczkowski RS, Ash DE (1994): Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors. Arch Biochem Biophys, 312, 31–37.
- Sepehrimanesh M, Aminlari M (2014): Arginase distribution in tissues of domestic avian species. Comp Clin Pathol, 23 (2), 353-356.
Abstract
Böbrek dokusundaki arginazın optimum şartları karaciğer arginazınınkinden farklı olabilir. Tavşan böbrek dokusundaki arginazın ölçülmesi için optimum şartlar tespit edilmediğinden böbrek dokusundaki arginazın optimize edilmesi ve karaciğer arginazınınki ile karşılaştırılması amaçlanmıştır. Çalışmada bir yaşında 6 adet Beyaz Yeni Zelanda Tavşanı’nın böbrek dokuları kullanıldı. Tavşan böbrek doku arginazı için preinkübasyon ısısı 53°C, preinkübasyon zamanı 15 dakika, inkübasyon zamanı 10 dakika, en uygun tampon NaHCO3-NaOH tamponu ve optimum pH 10.1 şeklinde tespit edilmiştir. Enzimin aktivitesi, 1 mM MnCl2 konsantrasyonunda en yüksek değere ulaşmıştır. Tavşan böbrek dokusu arginazının L-arginine karşı olan Km’i 12.5 mM olarak bulunmuştur. Enzimin aktive olması için Mn+2 iyonları ve 53 °C’ de preinkübasyon gereklidir. Böbrek arginazı için tayin edilen optimum şartlar karaciğer arginazınınkinden farklı olarak bulundu. Yapılan çalışma, ayrı gen lokusları tarafından kodlanan arginazların farklı optimum şatlara sahip olduğunu göstermektedir
Keywords
References
- Aminlari M, Shahbazkia HR, Esfandiari A (2007): Distribution of arginase in tissues of cat (Felis catus). J Feline Med Surg, 9 (2), 133-139.
- Benzer F, Temizer Ozan PS (2002): The levels of arginase enzyme activity in sheep with fasciolasis and some biochemical properties of arginase in liver tissue. FÜ Sağ Bil Vet Derg, 16 (2), 217-222.
- Colombo JP, Konarska L (1984): Arginase. In: Bergmayer GM. (Editor). Methods of Enzymatic Analysis. 3rd Edition, Weinheim: Vertag Chemie, 285-294.
- Dabir S, Dabir P, Somvanshi B (2005): Purification, properties and alternate substrate specificities of arginase from two different sources: Vigna catjang cotyledon and buffalo liver. Int J Biol Sci, 1 (3), 114-122.
- Dabir S, Dabir P, Somvanshi B (2006): The kinetics of inhibition of Vigna catjang cotyledon and buffalo liver arginase by L-proline and branched-chain amino acids. J Enzyme Inhib Med Chem, 21 (6), 727-731.
- Demir F, Ozan G, Temizer Ozan PS (2015): Ratlara uygulanan kurşun asetatın karaciğer arginazına etkisi ve enzimin bazı kinetik özellikleri. FÜ Sağ Bil Vet Derg, 29 (1), 37-43.
- Erdem N, Erişir M (2013): Tavşan Karaciğer Arginazının Optimize Edilmesi ve Dokulardaki Dağılımı. FÜ Sağ Bil Vet Derg, 27 (2), 81-86.
- Erişir M, Aydilek N, Aksakal M (2005): Effect of Vitamin E on Arginase Activity in the Liver and Kidneys of Testesterone Treated and Castrated Rabbits. Acta Vet Brno, 74, 527-531.
- Erişir M, Beytut E, Ozan TS, et al. (2003): Effects of dietary vitamin E and Selenium on Arginase Activity in the liver, kidney and heart of rats treated with high doses of glucocorticoids. Cell Biochem Funct, 21, 331-335.
- Erişir M, Erçel E, Yılmaz S, et al. (2005): Evaluation of optimal conditions for arginase activity in streptozotocin induced diabetic rats. Vet Med-Czech, 50, 69-76.
- Erişir M, Nazıroğlu M, Taşdemir B, et al. (2006): Effect of a dietary combined vitamin C and E supplementation on the liver, kidneys and brain arginase activity in non- pregnant and pregnant rats with streptozotocin-induced diabetes. Revue Med Vet, 157, 445-449.
- Erişir M, Tamser M, Taşdemir, et al. (2006): Ovariektomili Ratlara Estradiol 17-β ve Vitamin E Verilmesinin Arginaz Aktivitesi Üzerine Etkisi. Kafkas Üniv Vet Fak Derg, 12 (1), 31-35.
- Geyer JW, Dabich D (1971): Rapid method for determination of arginase activity in tissue homogenates. Anal Biochem, 39, 412-417.
- Glass RD, Knox WE (1973): Arginase isozymes of rat mammary gland, liver, and other tissues. J Biol Chem, 248, 5785-5789.
- Gotoh T, Sonoki T, Nagasaki A, et al. (1996): Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line. FEBS Lett, 395, 119-122.
- Guoyao WU, Morris SM (1998): Arginine metabolism: nitric oxide and beyond. Biochem J, 336, 1-17.
- Halifeoğlu İ (1993): İnsan Karaciğerinde, Eritrosit Ve Uterus Doku Arginazının Kinetik Özellikleri. Doktora Tezi, Elazığ Fırat Üniversitesi Tıp Fakültesi. Biyokimya Anabilim Dalı.
- Kadowaki H, Nesheim MC (1978): An assay for arginase in chicken kidney. Comp Biochem Physiol B, 61, 281–285.
- Kaysen GA, Strecker HJ (1973): Purification and properties of arginase of rat kidney. Biochem J, 133, 779- 788.
- Lowry OH, Rosenbrough NJ, Farr AL, et al. (1951): Protein measurements with the folin phenol reagent. J Biol Chem, 193, 265-275.
- Miyanaka K, Gotoh T, Nagasaki A, et al. (1998): Immunohistochemical localization of arginase II and other enzymes of arginine metabolism in rat kidney and liver. Histochem J, 30, 741–751.
- Powers GS, Meister T (1982): Urea synthesis and ammonia metabolism. In: Arias I, Popper H, Schachter D, Shafrits DA, editors: The liver: Biology and Pathobiology. Raven Press. New York, 251-263.
- Reczkowski RS, Ash DE (1994): Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors. Arch Biochem Biophys, 312, 31–37.
- Sepehrimanesh M, Aminlari M (2014): Arginase distribution in tissues of domestic avian species. Comp Clin Pathol, 23 (2), 353-356.
Details
| Primary Language | English |
|---|---|
| Subjects | Veterinary Surgery |
| Other ID | JA85SZ39DN |
| Journal Section | Research Article |
| Authors | |
| Publication Date | June 1, 2018 |
| Published in Issue | Year 2018 |