Study of Milking Efficiency, Biochemical Milk Composition and Hormonal Blood Parameters of Armenian Goat Breeds for the Second Lactation Period

Iranian Journal of Applied Animal Science

مقاله 14، دوره 3، شماره 1، خرداد 2013، صفحه 101-104   

نوع مقاله: Research/Original Article

نویسنده

G.Y. Marmaryan^*

Department of Biochemistry, Faculty of Veterinary and Animal Husbandry, Armenian State Agrarian University, Yerevan, Armenia

چکیده

The purpose of the given work was to study the dairy efficiency of the delivered, local and crossbreed goats in three different generations (F₁, F₂ and F₃), derived from their crosses, as well as the biochemical composition of milk and some bloodplasma hormones, participating in the process of lactopoez. For the biochemical tests of milk we have selected casein and serumproteins, iron in lactoferrin and xanthine oxidase activity as one of the enzymes of protein catabolism together with lysozyme activity.Deliveredgoat breeds surpassthe locals inmilk production. Cross-breeds F₁, F₂, and especially F₃ occupy an intermediate position, andthe latter ones even surpass Toggenburg breed, but are inferior to Alpine and Zaane breeds. It is stated a direct correlation between milk production of goat breeds and their crossbreeds and the level of prolactin in blood. It is noted the inverse correlation on the content of insulin.

کلیدواژه‌ها

casein؛ Goat؛ lactoferrin؛ lysozyme؛ xanthine oxidase

مراجع

Brundige D.R., Maga E.A., Klasing K.C. and Murray I.O. (2008). Lysozyme transgenic goats milk influences gastro-intestinal morphology in young pigs. J. Nutr. 138, 921-926.
Bulatov A.S. (2004). Constitutional, productivity and some biological features of Zaane goats for the different lactation. Ph D Thesis. Boil. Sci. Stavropol. Université de Gent, Belgique.
Cocorina E.P. (1996). Conditioned reflex and productivity of animals. Мoscow. Agropromizdat. 7, 196-202.
Deshmukh A.R., Donker J.D., Addis P.B. and Jenness R. (1989). Cellulose acetate and polyacrylamide gel electrophoresis for quantification of milk protein fractions. J. Dairy Sci. 72, 12-17.
Fedosimov V.A. and Cocorina E.P. (2000). Physiological and biochemical investigation of cows lactation. J. Zootechnics. 8, 21-28.
Galochkina V.P. and Galochkin V.A. (2008). About hypothetical mechanisms of biosynthesis and secretion of insulin in ruminant. J. Agricul. Biol. 6, 44-52.
Grachev I.I. (1995). Cell mechanisms of regulation milk secretion. Moscow, Elista. 5, 95-102.
Mollett T.A. and Malven P.V. (1982). Chronological profiles of prolactin and growth hormone in lactating cows. J. Dairy Sci. 65(2), 211-216.
Nevada V.E., Nikitin V.N. and Simirenko L.L. (1976). About age and breed features of insulin fluctuation in blood of calf. J. Phisiolog. 62, 1888-1891.
Scarlata R.W. (1962). A micromethod for determination of serum iron and binding capacity. J. Clin. Chem. 8(4), 360-369.
Schoonmarker J.P., Cecava V.M. and Faulkner D.B. (2003). Effect of source of energy and rate of growth on performance, carcass characteristics, ruminal fermentation, and serum glucose and insulin of early-weaned steers. J. Anim. Sci. 81(4), 843-855.
Selested M.E. and Martnez R.J. (1980). A simple and ultrasensitive enzymatic assay for the quantitive determination of lysozime in the pictogram range. J. Anim. Biochem. 109, 67-70.
Taranenko A.G. (1997). Physiological biochemical and molecular genetic basis of milk productivity increasing. Get. Sel. Evol. 14, 566-570.
Waud W.R. and Rajagopalan K.V. (1976). Xanthine oxidase assy. J. Arch. Biochem. Biophys. 172, 365-379.
Wolchover N. (2011). Cows make humanized milk. But is it safe? Life. Little Myst. 5, 21-28.