The Investigation on Interaction between Two Hepatic Enzymes and some Minerals in Broiler Chickens

Iranian Journal of Applied Animal Science

مقاله 26، دوره 4، شماره 4، اسفند 2014، صفحه 863-869   

نوع مقاله: Research/Original Article

نویسنده

A. Moharrery^*

Department of Animal Science, FacultyofAgricultur, Shahrekord University, Shahrekord, Iran

چکیده

The objectives of this study were to determinethe interactions between two hepatic enzymes and some minerals in the liver of broiler chickens. The study was performed with male and female from 1 to 56 days of age of broiler chickens. Malic acid was added to the water and offered to chickens freely from the start to the end of the experiment with constant concentration. The treatments consisted on zero (as a control), 0.05, 0.10 and 0.15% of malic acid which dissolved in water and given to them in waterer pan. The chicks were slaughter on 56 days old and liver enzymes including malate dehydrogenase (MDH) and isocitrate dehydrogenase (IDH) were measured on liver extract along with some mineral in dried liver. No significant difference (P>0.05) was observed between treatments for weight gain. Liver MDH activity did not show any significant difference, but IDH activity was increased (P<0.05) by malic acid consumption. Male chicks showed a 28% higher IDH-NADP activity in their liver compared to female chicks (P<0.05). Zinc and iron showed significant correlation with MDH and IDH, respectively. No significant negative correlation (P>0.05) was observed among mineral concentration in the chick liver and selenium concentration in the liver. However, it was found a significant positive correlation with concentration of lead, magnesium, nickel, manganese, mercury and cobalt in the chicken liver (P<0.05). In conclusion, malic acid administration to the water of chickens resulted in a linear accumulation of iron into the liver of them, butthere was not foundother mineral accumulation in this organ.

کلیدواژه‌ها

Broiler؛ enzyme interaction؛ IDH؛ MDH؛ mineral

مراجع

Abdullah N., Osman A.K. and Salaman K.A. (2010). Monitoring of aflatoxins and heavy metals in some poultry feeds. AJFS. 4, 192-199.
AOAC. (2000). Official Methods of Analysis. 17^th Ed. Association of Official Agricultural Chemists International. Gaithersburg, MD, USA.
Balnave D. (1975). The influence of essential fatty acids and food restriction on the specific activities of hepatic lipogenic and glutamate-metabolizing enzymes in the lying hen. Br. J. Nutr. 33, 439-445.
Bienfait H.F. (1996). Is there a metabolic link between H+ excretion and ferric reduction by roots of Fe-deficient plants – A viewpoint? J. Plant. Nutr. 19, 1211-1222.
Blonde D., Kresack E. and Kosicki G. (1967). The effects of ions and freeze-thawing on the supernatant and mitochondrial malate dehydrogenase. Can. J. Biochem. 45, 641-646.
Boling-Frankenbach S.D., Snow J.L., Parsons C.M. and Baker D.H. (2001). The effect of citric acid on the calcium and phosphorus requirements of chicks fed corn-soybean meal diets. Poult. Sci. 80, 783-788..
Brown D.G. and Burk R.F. (1973). Selenium retention in tissues and sperm of rats fed a torula yeast diet. J. Nutr. 103, 102-108.
Cheeseman A.J. and Clark J.B. (1988). Influence of the malate-aspartate shuttle on oxidative metabolism is a synaptosomes. J. Neurochem. 50, 1559-1565.
Djawdan M., Chippindale A.K., Rose M.R. and Bradley T.J. (1998). Metabolic reserves and evolved stress resistance in Derosophila melanogaster. Physiol. Zool. 71, 584-594.
Dousset J.C., Rioufol C., Philibert C. and P. Bourbon P. (1987). Effects of inhaled HF on cholesterol, carbohydrate and tricarboxylic acid metabolism in guinea pigs. Fluoride. 20, 137-141.
Edwards H.M. and Baker D.H. (1999). Effect of dietary citric acid on zinc bioavailability from soy products using an egg white diets with zinc sulfate hepatahydrate as the stander. Poult. Sci. 78, 113.
Ekmekci G., Somer G. and Sendil O. (2003). Simultaneous determination of copper, zinc and selenium in chicken liver by differential pulse polarography. Turk. J. Chem. 27, 347- 355.
Engle T.E., Nockels C.F., Kimberling C.V., Weaber D.L. and Johnson A.B. (1997). Zinc repletion with organic or inorganic forms of zinc and protein turnover in marginally zinc deficient calves.J. Anim. Sci. 75, 3074-3081.
Fleet J. and Salt D. (2009). Ionomics: mineral nutrition, physiology, and interactions as a biological system. J. Anim. Sci. 87, 370.
Goodridge A.G. and Ball O.(1967). Lipogenesis in the pigeon: in vivo studies. Am. J. Physiol. 213, 245-249.
Goodridge A.G. (1968). Conversion of [U14-C] glucose into carbon dioxide, glycogen, cholesterol and fatty acids in liver slices from embryonic and growing chicks. Biochem. J. 108, 655-661.
Gordon E., Newman C., Campbell A.M. and Williamson J.H. (2000). Purification and characterization of isocitrate dehydrogenase from Chlamydomonas reinhardtii. Department of Biology, Davidson College, Davidson.
Hill M. and Link J.E. (2009). Trace mineral interactions, known, unknown and not used. J. Anim. Sci. 87, 370.
Hoehl C., Oestreich R., Rosen P., Wiesner R. and Grieshaber M. (1987). Evidence for succinate production by reduction of fumarate during hypoxia in isolated adult rat heart cells. Arch. Biochem. Biophys. 259, 527-535.
Khan C.A. and Meijer G.A.L. (2005). The risk of contamination of food with toxic substances present in animal feed. Anim. Feed Sci. Technol. 133, 84-108.
Leveille G.A., O’Hea E.K. and Chakrabarty K. (1968). In vivo lipogenesis in the domestic chicken. Proc. Soc. Exp. Biol. Med. 128, 398-401.
Lowry O.H., Rosebrough N.J., Farr A.L. and Randall R.J. (1951). Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275.
Mc Donald P., Edwards R.A., Greenhalgh J.F.D., Morgan C.A., Sinclair L.A. and Wilkinson R.G. (2010). Animal Nutrition. Prentice Hall, Publisher.
Murakami K., Haneda M., Iwata S. and Yoshino M. (1997). Role of metal cations in the regulation of NADP-linked isocitrate dehydrogenase from porcine heart. Biometals. 10, 169-174.
Murakami K., Tsubouchi R., Fukayama M., Ogawa T. and Yoshino M. (2006). Oxidative inactivation of reduced NADP-generating enzymes in E. coli: iron-dependent inactivation with affinity cleavage of NADP-isocitrate dehydrogenase. Arch. Microbiol. 186, 385-392.
NRC. (1994). Nutrient Requirements of Poultry, 9^th Rev. Ed. National Academy Press, Washington, DC.
Nix J. (2002). Trace minerals important for cattle reproduction. http://www.sweetlix.com.
Ogawa T., Murakami K., Mori H., Ishii N., Tomita M. and Yoshin M. (2007). Role of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in E. coli. J. Bacteriol. 189, 1176-1178.
Rehman K., Andleeb S., Mahmood A., Bukhar S.M., Naeem M.M. and Yousaf K.(2012).Translocation of zinc and nickel from poultry feed to broilers and their excretion through litters. Global Vet. 8, 660-664.
Rikans L.E., Moore D.R. and Snowden C.D. (1991). Sex-dependent differences in the effects of aging on antioxidant defense mechanisms of rat liver. Biochim. Biophys. Acta. 1074, 195-200.
Romsos D.R. and Leveille G.A. (1974). Effect of diet on activity of enzymes involved in fatty acid and cholesterol synthesis. Adv. Lipid Res. 12, 97-146.
Rosebrough R.W., Mcmurtry J.P. and Vasilatos-Younken R. (1999). Dietary fat and protein interactions in the broiler. Poult. Sci. 78, 992-998..
SAS Institute. (2009). SAS®/STAT Software, Release 9.2. SAS Institute, Inc., Cary, NC.
Skinner J.T., Izat A.L. and Waldroup P.W. (1991). Fumaric acid enhances performance of broiler chickens. Poult. Sci. 70, 1444-1447.
Spears J.W. (2000). Micronutrients and immune function in cattle. Proc. Nutr. Soc. 59, 1-8.
Tanaka K., Ohtani S. and Shigeno K. (1983). Effect of increasing dietary energy on hepatic lipogenesis in growing chicks. I. Increasing energy by carbohydrate supplementation. Poult. Sci. 62, 445-451.
Thomassen Y. and Aaseth J. (1986). Selenium in human tissues. Pp. 33-105 in Occurrence and Distribution of Selenium. M. Ihnat, Ed. Boca. Raton, FL, CRC Press.
Varrone S., Consiglio E. and Covelli I. (1970). The nature of inhibition of mitochondrial malate dehydrogenase by thyroxine, iodine, cyanide, and molecular iodine. Eur. J. Biochem. 13, 305-310.
Wiesner R.J., Kreutzer U., Rosen P. and Grieshaber M.K. (1988). Subcellular distribution of malate-aspartate cycle intermediates during normoxia and anoxia in the heart. Biochim. Biophys. Acta. 936, 114-123.
Yamaguchi M., Kura M. and Okada S. (1982). Role of zinc as an activator of mitochondrial function in rat liver. Biochem. Pharmacol. 31, 1289-1293.