To establish the protocol of a standardized exercise test for evaluating exercise intolerance and degree of fitness in Thoroughbred racehorses, we examined serum lactate concentrations related to exercise intensities using the high speed tradmill. Twelve clinically healthy Thoroughbred racehorses with or without previous training or racing history were assigned to two groups, fit and unfit group, respectively. The protocol used for the standardized exercise test was consisted of two stages:stage ofwarm-up and that of acceleration. During the warm-up, the horses exercised 5 min at 1.8m/s and 3 min 3.4m/s without inclination. At the acceleration stage, exercise test was performed at 10% slope and the speed was increased from the initial 5m/s to the maximal speed which each tested horse could keep up with. The speed was increased with incremental steps of 1 m/s every minute. During the last 15 sec of each step, blood samples were collected for serum lactate determination. V max (masimal treadmill speed which tested horses could keep up with) of the fit group (10.93+_0.33m/s, mean+_SE, n=6) was higher than that of the unfit group (9.52+_0.23m/s, mean+_SE, n=6). Serum lactate concentrations increased exponentially according to exercise intensities. V la4 (speed producing a serum lactate concentration of 4mmol/l) of the fit group, 6.45+_0.26m/s, was higher than that of the unfit group, 5.45+_0.23m/s. La peak (peak plasma lactate concentration during the exercise test) was lower in the fit group (20.34+_1.62mmol/l at 1 min after maximal intensity exercise) than in the unfit group (24.78+_1.09mmol/l at 2 min after maximal exercise step). t50% (time required for the recovery of lactate concentration to be one-half of La peak after maximal exercise) of the unfit group and the fit group were 40.0 and 18.0 min, respectively. Therefore, the protocol of the incremental standardized exercise test utilized in this study seems to be reliable for the assessment of fitness and exercise intolerance for the Thoroughbred racehorses.

Ceruloplasmin (Cp) was isolated from fresh equine plasma by precipitation, cellulose chromatography, and improved ion-exchange chromatography. Purified equine Cp is a glycoprotein having a molecular weight of approximately 115,000. In electrophoresis, equine Cp migrated to the alpha 1-globulin region, its isoelectric point was about 4.15 and consisted of about 890 amino acid residues. Serum Cp concentration was measured by use of the single radial immunodiffusion method. In clinically normal horses, the mean (+/- SD) serum Cp concentration of newborn foals was 2.87 +/- 0.40 mg/ml and that of 3-month-old foals was 5.02 +/- 0.92 mg/ml, which was similar to the adult value. It reached a peak of 6.06 +/- 0.74 mg/ml in 2-year-old horses. The Cp concentration in mares was not statistically different for the perinatal period, but it decreased immediately before and after delivery. Concentration of Cp increased at 6 days after IM administration of turpentine oil, castration, or jejunojejunostomy in adult horses, and increased to peak values twice as high as baseline values at 7 to 14 days, returning to baseline values at 28 days after treatment. We concluded that equine serum Cp is an acute-phase reactive protein increased in the intermediary or later phase of acute inflammation.

Concentration of hyaluronate (HA) in equine serum was determined by a recently developed specific radioassay. The mean +/- SD HA concentration in equine serum was 288 +/- 145 micrograms/L, was age dependent, and varied widely between horses (range, 190 to 760 micrograms/L). Light or moderate exercise increased serum HA concentration from baseline values by 1.5- to 3-fold. In all horses, serum HA concentration returned to or below the original resting values 1 and 2 hours after exercise.

To establish whether Mycobacterium paratuberculosis could be cultured from Dulbecco phosphate-buffered saline solution (DPBSS) and to test 3 sampling methods, DPBSS supplemented with 2% fetal bovine serum was inoculated with M paratuberculosis at concentrations of 10(4), 10(3), 10(2), 10(1), and 10(0) colony-forming units/ml. The inoculated media was sampled after mixing, after centrifugation, and after centrifugation and decontamination with 0.75% hexadecylpyridinium chloride. The samples were inoculated onto 3 slants of Herrolds egg yolk medium supplemented with sodium pyruvate and mycobactin J and 1 slant without mycobactin J. Mycobacterium paratuberculosis was isolated following all 3 sampling methods for all concentrations. Treatment with hexadecylpyridinium chloride decreased the number of colonies isolated. To test the efficacy of a 10-step wash procedure for removing M paratuberculosis from bovine ova, washed zona pellucida intact bovine ova were incubated in DPBSS supplemented with 2% fetal bovine serum containing concentrations of 10(4), 10(3), 10(2), 10(1), and 10(0) colony-forming units of M paratuberculosis/ml for 12 hours at 22 C. Ten zona pellucida intact ova were removed from each concentration and washed by passing through 10 changes of DPBSS supplemented with 15% fetal bovine serum. The media from each wash step was inoculated onto slants of Herrolds egg yolk medium. The ova were included with the tenth wash step. Mycobacterium paratuberculosis was isolated from 1 of 10 tenth-wash steps at the 10(4) concentration and 5 of 10 tenth-wash steps at 10(3).

We used size-exclusion high-performance liquid chromatography (HPLC) to investigate the properties of the 2 isoforms of vitamin A-containing (holo) retinol-binding protein (RBP) in animals: the form that is bound to transthyretin (holo-TTR-RBP), and the form that does not bind to TTR (holo-free RBP). We also used radial immunodiffusion to measure immunologically active RBP (apo+ holo RBP). We compared the isoforms of RBP in animals with those of human beings to determine which animal is the best model of human RBP. Size-exclusion HPLC detected holo-free and holo-TTR-RBP in every animal species studied. Apparent concentration of holo-TTR-RBP varied among species: that of rabbits and dogs much greater than that of apes, sheep, goats, monkeys, rhinoceroses, felids, rats, human beings, and deer greater than that of pigs, zebra, and bison greater than that of penguins. Dogs have unusual RBP chromatograms; they have high concentration of RBP, but also appear to transport much of their vitamin A on proteins other than RBP, Human RBP antibody preparations could detect apo + holo RBP immunologic activity only in apes, monkeys, and felids. Apes and monkeys appeared to have complete cross-reactivity to human RBP antibodies. Felids may have substantial, but partial, cross-reactivity. Apes and monkeys appear to be the most relevant animal models for study of human RBP transport. However, there is a need for less-expensive models. Further research is needed, but in the interim, rats or sheep may be satisfactory for some purposes.

Six nontrained mares were subjected to steady-state, submaximal treadmill exercise to examine the effect of exercise on the plasma concentration of atrial natriuretic peptide (ANP) in arterial, compared with mixed venous, blood. Horses ran on a treadmill up a 6 degree grade for 20 minutes at a speed calculated to require a power equivalent to 80% of maximal oxygen uptake. Arterial and mixed venous blood samples were collected simultaneously from the carotid and pulmonary arteries of horses at rest and at 10 and 20 minutes of exercise. Plasma was stored at -80 degrees C and was later thawed; ANP was extracted, and its concentration was determined by radioimmunoassay. Exercise caused significant (P < 0.05) increases in arterial and venous plasma ANP concentrations. Mean +/- SEM arterial ANP concentration increased from 25.2 +/- 4.4 pg/ml at rest to 52.7 +/- 5.2 pg/ml at 10 minutes of exercise and 62.5 +/- 5.2 pg/ml at 20 minutes of exercise. Mean venous ANP concentration increased from 24.8 +/- 4.3 pg/ml at rest to 67.2 +/- 14.5 pg/ml at 10 minutes of exercise and 65.3 +/- 13.5 pg/ml at 20 minutes of exercise. Significant differences were not evident between arterial or mixed venous ANP concentration at rest or during exercise, indicating that ANP either is not metabolized in the lungs or is released from the left atrium at a rate matching that of pulmonary metabolism.

In present day, supplementation of extra minerals and vitamins is highly essential in commercial diets due to high productivity and to withstand the detrimental effects of different stresses. Selenium is one of essential trace minerals for better growth and productivity as well as anti-stressor in commercial broilers. Nano-selenium can effectively be synthesized through High Energy Ball Milling (HEBM) technique from its precursor, for use in commercial broilers as anti-stressor and to support multiple bodily functions. The prepared nano particle had 44.5 % of selenium as measured by Energy Dispersive X-ray (EDAX) analysis with the product yield of 50 g/hr. The chemical composition of sodium selenite powder was same as that of the original mega particle. The size of Se nano particle ranged from 37-85 nm as analyzed through Field Emission Scanning Electron Microscope (FESEM). X-Ray diffraction pattern confirmed that the synthesized Se nano particle was free of impurities and provided accurate information on the atomic arrangements. The Fourier Transform Infra-Red (FTIR) spectrum of synthesized nano particle source of selenium peaks was located at 3023.26, 2800.12, 2502.23, 2314.17, 1610.40 and 1413.30 cm-1 which showed chemical bonding in a target material. The zeta potential of nano selenium was -23.30 mV when analyzed through particle size analyzer. Se nano-particles could be successfully synthesized through High Energy Ball Milling method from its precursor and could be characterized for its quantity, size, shape, stability and purity. The synthesized Se nano-particles could be utilized for the conduct of biological trial in commercial broilers.

The present study reports the concentration of Copper, Zinc, Iron and Manganese in the blood plasma of male kutchi camels during their breeding season. The respective concentrations of the plasma trace minerals were 112.94 ±O.44, 105.65±2.08, 117.65±1.72 and 160.29±0.75 µ/dl.