Vet Med - Czech, 2005, 50(2):69-76 | DOI: 10.17221/5598-VETMED
Evaluation of optimal conditions for arginase activity in streptozotocin induced diabetic rats
- 1 Department of Biochemistry, Veterinary Faculty of Firat University, Elazig, Turkey
- 2 Province Veterinary Control Laboratory, Elazig, Turkey
The assay conditions needed to achieve maximal activity of liver and kidney arginase in diabetic and non-diabetic rats were investigated and compared. The physicochemical and kinetic properties of liver arginase in diabetic and control rats were very similar, those of kidney arginase were significantly different. It was found that preincubation temperature (68°C), preincubation period (20 min), optimum pH (10.1) of liver arginase and Km (3.2) for its substrate, L-arginine, did not change in diabetic and non-diabetic rats. As a consequence of diabetes, the optimum Mn2+ concentration for liver arginase only changed from 1 to 2 mM. Although the preincubation temperature and period for activation of kidney arginase in control rats was unnecessary, they were found to be 56ºC and 12 min in diabetic rats. The pH profile of arginase in kidney of diabetic rats was different from that of control rats. The Km value (6.7) of arginase for L-arginine in kidney is unchanged in diabetes whereas a marked decrease in Vmax was found. Optimum Mn2+ concentration (2 mM) for kidney arginase was unchanged in diabetes. The activity of arginase in liver of diabetic animals was higher 1.5 to 1.7 times than that of controls. Diabetes caused an about 53% decrease of arginase activity in kidney of female rats, 26% in that of males. These findings may suggest an idea that encoded arginases by separate gene loci may be affected differently by the pathological and hormonal status.
Keywords: arginase; diabetes; physicochemical and kinetic properties
Published: February 28, 2005 Show citation
References
- Aminlari M., Vaseghi T. (1992): Arginase distribution in tissue of domestic animals. Comparative Biochemistry and Physiology B, 103, 385-389.
Go to original source...
Go to PubMed...
- Baxter L.C.A., Schofield P.J. (1980): The effects of a high fat diet on chronic streptozotocin-diabetic rats. Diabetologia, 18, 239-245.
Go to original source...
Go to PubMed...
- Bond J.S. (1973): Effect of manganese and amino acids on proteolytic inactivation of beef liver arginase. Biochimica et Biophysica Acta, 327, 157-165.
Go to original source...
Go to PubMed...
- Bond J.S., Failla M.L., Unger D.F. (1983): Elevated manganese concentration and arginase activity in livers of streptozotocin-induced diabetic rats. Journal of Biological Chemistry, 258, 8004-8009.
Go to original source...
- Bond J.S., Unger D.F., Garganta C.L. (1986): Properties and regulation of mouse liver arginase. In: Schramm V.L., Wedler F.C. (eds.): Manganese in Metabolism and Enzyme Function. Academic Press, London and New York. 239-257.
Go to original source...
- Erisir M., Ozan T.S. (1999): Some properties of purified and non-purified rumen tissue arginase in cattle (in Turkish). Turkish Journal of Veterinary and Animal Sciences, 23, 597-608.
- Failla M.L. (1986): Hormonal regulation of manganese metabolism. In: Schramm V.L., Wedler F.C. (eds.): Manganese in Metabolism and Enzyme Function. Academic Press, London and New York. 93-105.
- Geyer J.W., Dabich D. (1971): Rapid method for determination of arginase activity in tissue homogenates. Analytical Biochemistry, 39, 412-417.
Go to original source...
Go to PubMed...
- Glass R.D., Knox W.E. (1973): Arginase isozymes of rat mammary gland, liver, and other tissues. Journal of Biological Chemistry, 248, 5785-5789.
Go to original source...
- Green M., Miller L.L. (1960): Protein catabolism and protein synthesis in perfused livers of normal and alloxan-diabetic rats. Journal of Biological Chemistry, 235, 3202-3208.
Go to original source...
- Grofte T., Jensen D.S., Gronbaek H., Wolthers T., Jensen S.A., Tygstrup N., Vilstrup H. (1998): Effects of growth hormone on steroid-induced increase in ability of urea synthesis and urea enzyme mRNA levels. American Journal of Physiology, 275, E79-E86.
Go to original source...
Go to PubMed...
- Haggerty D.F., Spector E.B., Lynch M., Kern R., Frank L.B., Cederbaum S.D. (1983): Regulation expression of genes for enzymes of the mammalian urea cycle in permanent cell-culture lines of hepatic and non-hepatic origin. Molecular and Cellular Biochemistry, 53/54, 57-76.
Go to original source...
Go to PubMed...
- Hirsch-Kolb H., Kolb H.J., Greenberg D.M. (1971): Nuclear magnetic resonance studies of manganese binding of rat liver arginase. Journal of Biological Chemistry, 246, 395-401.
Go to original source...
- Husson A., Buquet C., Vaillant R. (1987): Induction of the five urea-cycle enzymes by glucagon in cultured foetal rat hepatocytes. Differentiation, 35, 212-218.
Go to original source...
Go to PubMed...
- Jenkinson C.P., Grigor M.R. (1994): Rat mammary arginase: isolation and characterization. Biochemical Medicine and Metabolic Biology, 51, 156-165.
Go to original source...
Go to PubMed...
- Jorda A., Cabo J., Grisolia S. (1981): Changes in the levels of urea cycle enzymes and in metabolites thereof in diabetes. Enzyme, 26, 240-244.
Go to original source...
Go to PubMed...
- Junod A., Lambert A.E., Orci L., Pictet R., Gonet A.E., Renold A.E. (1967): Studies on the diabetogenic action of streptozotocin. Proceedings of the Society for Experimental Biology and Medicine, 126, 201-205.
Go to original source...
Go to PubMed...
- Kadowaki H., Nesheim M.C. (1978): An assay for arginase in chicken kidney. Comparative Biochemistry and Physiology B, 61, 281-285.
Go to original source...
Go to PubMed...
- Kaysen G.A., Strecker H.J. (1973): Purification and properties of arginase of rat kidney. Biochemical Journal, 133, 779-788.
Go to original source...
Go to PubMed...
- Konarska L., Tomaszewski L. (1975): Studies on L-arginase the small intestine. Biochemical Medicine, 14, 250-262.
Go to original source...
Go to PubMed...
- Lowry O.H., Rosenbrough N.J., Farr A.L., Randall R.J. (1951): Protein measurements with the folin phenol reagent. Journal of Biological Chemistry, 193, 265-275.
Go to original source...
- McLean P., Novello F. (1965): Influence of pancreatic hormones on enzymes concerned with urea synthesis in rat liver. Biochemical Journal, 94, 410-422.
Go to original source...
Go to PubMed...
- Pfaffly J.R. (2001): Diabetic complications, hyperglycemia & free radicals. In: http://www.medicine.uiowa.edu/frrb/education/FreeRadicalSp01/Paper%205/PfafflyJ-Paper%205.pdf
- Powers G.S., Meister T. (1982): Urea synthesis and ammonia metabolism. In: Arias I., Popper H., Schachter D., Shafrits D.A. (eds.): The Liver: Biology and Pathobiology. Raven Press, New York. 251-263.
- Reczkowski R.S., Ash D.E. (1994): Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors. Archives of Biochemistry and Biophysics, 312, 31-37.
Go to original source...
Go to PubMed...
- Upadhyaya S.K.C., Baquer N.Z. (1996): Effects of vanadate and insulin on the activities of selected enzymes of amino acid metabolism in alloxan diabetic rat kidney. Biochemistry and Molecular Biology International, 40, 853-860.
Go to original source...
Go to PubMed...
- Upadhyaya S.K.C., Raju J., Baquer N.Z. (1999): Modulation of mRNA levels of liver arginase by insulin and vanadate in experimental diabetes. Indian Journal of Biochemistry and Biophysics, 36, 125-128.
- Schimke R.T. (1962): Adaptive characteristics of urea cycle enzymes in the rat. Journal of Biological Chemistry, 237, 459-468.
Go to original source...
- Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W. (1997): Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function. Biochemistry, 36, 10558-10565.
Go to original source...
Go to PubMed...
- Spector E.B., Rice S.C.H., Moedjono S., Bernard B., Cederbaum S.D. (1982): Biochemical properties of arginase in human adult and fetal tissues. Biochemical Medicine, 28, 165-175.
Go to original source...
Go to PubMed...
- Spolarics Z., Bond J.S. (1989): Comparison of biochemical properties of liver arginase from streptozocin-induced diabetic and control mice. Archives of Biochemistry and Biophysics, 274, 426-433.
Go to original source...
Go to PubMed...
- Tarrab R., Rodriguez J., Huitron C., Palacios R., Soberon G. (1974): Molecular forms of rat-liver arginase. Isolation and characterization. European Journal of Biochemistry, 49, 457-468.
Go to original source...
Go to PubMed...
- Van Elsen A.F., Leroy J.G. (1975): Arginase isoenzymes in human diploid fibroblasts. Biochemical and Biophysical Research Communications, 62, 191-198.
Go to original source...
Go to PubMed...
- Winegrad A.I. (1987): Does a common mechanism induce the diverse complications of diabetes? Diabetes, 36, 396-406.
Go to original source...
Go to PubMed...
This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International (CC BY NC 4.0), which permits non-comercial use, distribution, and reproduction in any medium, provided the original publication is properly cited. No use, distribution or reproduction is permitted which does not comply with these terms.