Search

The response to transport stress of serum GOT, LDH, and ALD was studied in 35 heads of cattle, aged 18 months to 20 years. The influence of different factors upon serum enzyme behaviour in cattle after exposure to transport stress was tested by means of mathematico-statistical methods. The following conclusions were drawn: 1. Transport stress on cattle was followed by rise in GOT, LDH, and ALD activities in serum. 2. The strongest rise was recorded from ALD activity and the smallest from LDH. 3. All three serum enzymes continued to rise up to the time of slaughter (20 to 50 hours after transport). 4. The enzyme activities recorded from blood after slaughter did not differ significantly from those in venous blood. 5. Intensity of ALD activity rise was found to depend on the transport distance (if it was more than 20 km), age of animal, and ambient temperature. 6. The rise in GOT activity was found to depend only on the given ambient temperature. 7. The behaviour of LDH activity did not reveal any secured relationship with any of the examined factors (transport distance, age keeping, and tuberculosis state or ambient temperature).

Significant rise of fructose in the blood plasma of cattle resulted from an application of sorbite solution (0.5 g sorbite per kg live weight), with its onset as early as during the infusion. The highest concentration was reached 15 minutes after completion of infusion. Rise in glucose (11 mg/100 ml plasma on average) failed to prove statistically significant and dropped temporarily (after 60 to 120 minutes) below the original value. The lactate level in the blood went up temporarily and reached its maximum 30 minutes from the end of infusion. Sorbite solution (1 g/kg live weight) was intravenously applied to sheep and tock fructose to its maximum after 30 minutes. Intraperitoneal application of sorbite solution (1 g/kg live weight) was tolerated well also by piglets and triggered an age-dependent decline of glucose in blood plasma.

Horses were examined for the behaviour of various blood constituents prior to and following infusions of solutions of glucose, fructose, invertose, and sorbitol. Infusion of 0.5 g/kg live weight glucose to six horses was followed by half-life variation between eleven and 23 minutes. Subsequent infusion of invertose to the same animals usually caused prolongation of glucose half-life. Half-life values were between 17 and 33 minutes for fructose and between 21 and 80 minutes for glucose. Infusion of 0.5 g/kg live weight fructose to two horses was followed by half-life values between 17 and 18 minutes, while the half-life values of sugar alcohol were 16, 16, 27, and 29 minutes in four horses who had received sorbitol. Sugar or sorbitol infusion was not followed by substantive change of lactate and pyruvate concentrations in the blood or free fatty acids in the blood plasma or GOT activity. The rise of insulin in the blood plasma was differentiated. Invertose and sorbitol solutions, consequently, can be recommended for application to horses.

Acid phosphatase of erythrocytes of several species was investigated, with three isozymes having been recorded from swine (three types), three (two types) from horse, four (one type) from dog, two (two types) from cat, two (three types) from duck, and two (one type) from fowl. The Michaelis constant of the enzyme varied between 3.5 and 5 X 10(-4) M for the species involved. The species, however, differed slightly for the optimum pH of the enzyme. The average enzymatic activities were (5.68 +/- 0.42 for dog, 4.46 +/- 1.0 for horse, 3.8 +/- 0.24 for swine, 3.72 for cat, 2.5 +/- 0.62 for duck, and 1.9 +/- 0.8 for fowl. All values are units per gram haemoglobin. Even relatively low concentrations (0.2 or 1 mM) of copper, mercury, and cadmium ions were found to be strong inhibitors of the acid erythrocyte phosphatase.

Glucose and fructose half-lives following intravenous infusion of 1.0 or 0.5 g/body weight invertose solution (200 g/l) were established in six Beagle dogs. The average half-lives measured were 7.8 for glucose (variation between 6.0 and 13.5) and 7.5 for fructose (variation between 4.5 and 11.0), all values given in minutes. Administration of invertose instead of glucose for parenteral energy supply proved favourable in various respects. Infusion of invertose was temporarily followed by rises within physiological limits of lactate and pyruvate in the blood and of insulin concentrations in the blood plasma, whereas the levels of free fatty acids declined. A 25-per-cent fructose solution was infused (0.5 g/kg body weight) to three dogs, and the half-lives then measured were six, nine, and 13 minutes. The insulin concentration rose temporarily, while the free fatty acids went down. The same doses of sorbite gave half-lives of 15.5 or 17 minutes. Infusion was followed by temporary increase of fructose and insulin in the blood plasma.

Monosaccharides were intravenously injected to eight adult heads of cattle, between 380 kg and 670 kg in live weight, to study, in the context of stress endurance, the half-life values of the sugars as well as monosaccharide effects upon concentrations of various blood components. The fructose concentration in the blood plasma went up temporarily following the infusion of glucose solution. Fructose infusion usually caused only little rise of the glucose concentration in blood plasma, with hypoglycaemia occurring quite often towards the end of an experimental period. The half-life values of sugar in blood plasma were between twelve and 29 and those of fructose between ten and 17 minutes. The rate of fructose conversion was higher than that of glucose conversion, but values were identical in some cases. The pyruvate concentration in the blood and the insulin level in blood plasma went up in response to infusion of monosaccharide solutions. Urine excretion of monosaccharides following invert sugar infusion was less than half of that in response to glucose infusion.

The properties of fructose-1.6-disphosphatase in supernatant of homogenate of liver, kidneys, and adductor muscles of cattle were tested. EDTA was found to activate the enzyme up to concentrations of 10 mMol. The pH optimum was 7.5 in the presence of EDTA. Even lower concentrations of magnesium ions caused activation of the enzyme, but an activating effect was obtained as well from relatively high Mg concentrations. Fructose-1.6-diphosphatase could by activated also by 0.2 mMol Mn or Co ions or 1 mMol Zn ions. Inhibitive action was obtained from Cu, Cd, Pb, and Hg ions. Microsomal fractions of cattle liver and kidney caused high activity of glucose-6-phosphatase, but only low action was obtained be using microsomal fractions of mesenteric mucous membrane or brain. Mg ions, basically, failed to trigger activation, and higher concentrations even caused inhibition. The relatively high activity of both fructose-1.6-diphosphatase and glucose-6-phosphatase in kidney of cattle appeared to suggest an involvement of those enzymes in gluconeogenesis.

Different quantities of sorbite-electrolyte solution were intravenously administered to eight heads of cattle and four heads of sheep (application values being 50 g sorbite, 0.3049 g MgCl2-6H2O, 0.3728 g KCl, 0.5477 g CaCl2-6H2O, 5.265 g NaCl, 6.804 g sodium acetate-3H2O with 1,000 ml distilled water). Different rises of sorbite, fructose, and glucose were recorded from the blood plasma. Certain manifestations of incompatibility and intolerance phenomena were observed, among them increase of cardiorespiratory activity and muscular tremor. Those findings were obtained primarily from animals which exhibited also strong rise in glucose concentration. One of the sheep died. Larger quantities of solution (2,000 ml or 4,000 ml) were intraperitoneally applied to ten heads of cattle and tolerated by them with no reaction. Sorbite in blood plasma usually reached its maximum two or three hours from application, however, without any rise of fructose or glucose. Slow drip infusion or intraperitoneal infusion are the techniques recommended for application of the above sorbite-electrolyte solution to ruminants.

Behaviour of Mg and Ca content in the blood serum of 28 cattle with grass tetany and hypocalcaemia was evaluated at short time intervals after infusion of 500 ml of a solution A (containing 12 g Mg-adipat and 5 g Ca-gluconate/100 ml aqua dest.) and a solution B (containing 12 g Mg-adipate and 12 g Ca-gluconate/100 ml) respectively. After treatment with the last-named solutions there was evident a considerable increase of Mg-values in the blood serum for a longer period (up to 6 h), also in the case of distinct hypomagnesaemia while Ca-values of the circulating blood declined more quickly. Efficacy of treatment was the better the earlier infusion was performed after occurence of clinical signs. Application of solution B for treatment of grass tetany and paresis with tetany like symptoms is recommended for several reasons. Necessity of assurance the Mg and Ca supply after infusion is emphasized.

The activity of acid phosphatase in the testicular parenchyma of cattle was found to be higher than that in the endometrium. The acid phosphatase of either tissue broke up p-nitrophenylphosphate at a rate twice as high as that reached for di-sodium phenylphosphate. Hydrolysis of phenolphthalein diphosphate was slower and that of beta-glycerophosphate very slow. Two optimum pH values and two isozymes were recordable from acid phosphatase in testicular supernatant and three optimum pH values as well as three isozymes from that in endometrial supernatant. Even concentrations pf 0.2 mM of copper and mercury ions were strongly inhibiting the acid phosphatase, whereas lead and cadmium ions proved less effective. The activity of acid phosphatase from testes dropped by 24 per cent and that from the endometrium by 16 per cent over eight weeks of storage at -20 degrees C. The average activity of alkaline phosphatase in the endometrium was much higher than that in testicular parenchyma. Alkaline phosphatase from testes exhibited the shortest break-up time for p-nitrophenylphosphate, whereas disodium-phenylphosphate was broken up at the highest rate by endometrial alkaline phosphatase. Two isozymes of alkaline phosphatase were recordable each from the testes and endometrium.

Studies into the activity of adenosine triphosphatase (ATPase) in homogenates of liver, cerebral cortex, renal cortex, and mucosa of small intestine of swine have shown differentiated activity patterns, with peak activity developing in the liver. This has been related to a particularly high metabolism performance of the liver in fattening pigs. No difference was found to exist between magnesium activation of ATPase of swine tissue homogenates and that in tissue obtained from ruminants. ATPase which could be activated by sodium and potassium ions and inhibited by ouabain was detectable from cerebral and renal cortex. Sodium and potassium ATPases accounts from some 25 per cent of the total activity. ATPase that could be stimulated by calcium ions was recorded only from liver homogenate. The optimum pH values of ATPase were between 7.5 and 8 in the liver, 9 in mucosa of small intestine, and 9.5 in cerebral and renal cortex.

Studies conducted into the activity of adenosine triphosphatase (ATPase) in homogenate of several tissues of sheep and against the background of pH 7.5 (tris-HCl buffer) have shown highest enzyme activity to develop in renal cortex and cerebral cortex followed, in declining order of quotation, by liver, myocardium, and mucous membrane of small intestine. ATPase activities were studied also in the presence of pH-values between 7.2 and 8.95 (tris-HCl buffer) and between 8.6 and 11 (piperazine buffer), with the pH optimum of ATPase in the above tissues having been found to lie at approximately 9.0. Different concentrations of Mg ions were added, and maximum ATPase activity of 2 mMol ATP was obtained by adding 2 mMol Mg. Decline in ATPase activity should be expected in the case of hypomagnesaemia. Addition of different concentrations of sodium and potassium ions gave in most of the tissues tested maximum activity in response to 10 mMol potassium and 68 mMol sodium. Na-K ATPase could be inhibited by oubain particularly in cerebral and renal cortex.

Monosaccharide half-life as well as the effects of intravenous infusion of 0.5 g/kg body weight glucose, fructose, and invert sugar solutions on insulin levels in blood plasma as well as on pyruvate and lactate concentrations in the blood were measured in two adult sheep weighing 72 kg and 65 kg. The half-life values for glucose were 16 minutes and 19 minutes and that for fructose 20 minutes. Glucose half-life, following infusion of invert sugar, was 35 minutes or 25 minutes, while that of fructose was 16 minutes in either case. Infusion of fructose solution was followed by a somewhat sizeable and prolonged rise of the glucose levels in blood plasma. Infusion of glucose solution resulted only in short-time increase of fructose concentrations in blood plasma. The highest insulin rise in blood plasma was found to have taken place in response to infusion of fructose solution. Pyruvate and lactate concentrations underwent merely minor changes. Reference is made to the potential benefit of using invertose solution in the treatment of ketosis (cf. second communication).