Activity and properties of adenosine triphosphatase in erythrocytes and various tissues (brain, liver, kidney, small intestine mucosa) of cattle]

In 15 samples of haemolysate of bovine erythrocytes, the splitting of phosphate from adenosine triphosphate average 158 +/- 63 X 10(-3) muMol/min/g haemolysate haemoglobin. Estimation of total adenosine triphosphatase in homogenates of various organs from cattle showed that spleen, liver, kidney and brain possessed high activity, while the activity was moderate in lung, myocardium and skeletal muscle, and low in endometrial mucosa and spinal cord. There was a relatively large proportion of Na-K-adenosine triphosphatase in brain and kidney. In various organs the activity of the enzyme was dependent upon the concentrations of Mg, Na, K and Ca. The inhibition of adenosine triphosphatase in various tissues by ouabain was studied. The optimum pH for the enzyme lay in the weakly alkaline region.     

Activity and properties of alkaline phosphatase in the plasma and various organs (kidney, liver, small intestine mucosa, bone) of the swine]

There was a high activity of alkaline phosphatase in the blood plasma of piglets during the first few days of live; enzyme obtained at this time had high heat stability and was readily inhibited by L-phenylalanine (5 mM). The enzyme in blood was inhibited to a greater extent than alkaline phosphatase from intestinal mucosa. With increasing age there was a fall in heat stability and in the ease with that the enzyme could be inhibited by phenylalanine. The proportion of alkaline phosphatase derived from bone and present in blood plasma increased with increasing age. Two isoenzymes were detected in liver, kidney, lung, intestinal mucosa and endometrial mucosa by electrophoresis in polyacrylamide gel. Heat lability and inhibition by phenylalanine were good criteria for differentiating different types of alkaline phosphatase in pigs. In the case of alkaline phosphatase in blood plasma, disodium phenylphosphate was split more readily than p-nitrophenyl phosphate and very much more readily than phenolphthalein diphosphate and beta-glycerophosphate.     

The activity and properties of fructose-1,6-diphosphatase in various tissues (Liver, Kidneys, skeletal muscle, small intestine mucosa) in swine]

The following parameters are recommended for activity determination of FDPase by release of inorganic phosphate at 37 degrees C of enzyme from liver and kidneys of swine: pH 7.5, 2 mMol concentration of fructose-1,6-diphosphate, 5 mMol concentration of Mg ions, and ten minutes of incubation. When the activity of FDPase was analysed with temperatures of 22 degrees C, and 45 degrees C, rises were recorded up to the highest temperature. ADTA was strongly activating along with 2 mMol of Mg ions in a test arrangement of 5 mMol concentration. Manganese, zinc, and cobalt ions are strong activators even in low concentrations (0.2 or 1.0 mMol), whereas copper, cadmium, and mercury ions are strong inhibitors of the enzyme. Average activities of FDPase were analysed by means of the optical test in the liver and kidneys of fetuses aged 98 days. They were 1.79 or 0.38 units in one gram of tissue. In pigs for slaughter they had been 2.06 or 3.58 units in one gram of tissue.     

Studies on activity and properties of alkaline phosphatase in body fluids (plasma, serum, bile) and in various organs (kidney, liver, small intestine, bones) in cattle]

Behaviour of the alkaline phosphatase (AP) present in blood serum, blood plasma, bile and extracts of organs (kidney, liver, intestinal mucosa, bone) was studied under various conditions of incubation (after preliminary heat treatment and after addition of L-phenyl-alanine). AP in serum and bile from calves and bullocks was very heat labile and did not inhibit phenylalanine much. EDTA and citrate were active inhibitors of AP, and therefore blood samples containing these anticoagulants are unsuitable for enzyme investigations. Out of four compounds tested, the substrate that was most rapidly split by AP from tissues was disodium phenylphosphate. AP activity was particularly high in kidney. The most heat-labile form of AP was that present in bone. AP in different tissues was inhibited to different extents by phenylalanine.     

Histochemistry of acid phosphatase in small intestine mucosa in experimental coccidiosis in suckling piglets]

The activity of acid phosphatase (phosphohydrolase of orthophosphate monoesters; EC. 3.1.3.2) was evaluated densitometrically in the mucosa of duodenum, jejunum and ileum of 22 conventional piglets which were experimentally infected by oocysts of the coccidiae Isospora suis (infection dose of 200,000 oocysts) on day one after parturition (DAP). The activity of the studied hydrolase was investigated in the infected piglets during days two to ten after infection (DAI) in the intestinal mucosa (enterocytes) and in goblet cells. The density of the reaction product of acid phosphatase was simultaneously determined in the same mucosal cells of different sections of the small intestine in five control conventional piglets at the age of 2-14 days. In the small intestine mucosa of control piglets the activity of acid phosphatase was demonstrated to be located especially in the supranuclear zone of enterocytes. As for goblet cells, the reaction product of acid phosphatase is distributed in all zones (supra-, para-, infranuclear zones); the lowest density of this enzyme was found in the infranuclear zone. The activity of acid phosphatase is also localized in intestinal crypts: in their cells the enzyme concentration is decreasing from duodenum to caudal sections. Important changes were revealed, in comparison with the control data, in the development of the activity of acid phosphatase in the intestinal mucosa cells in the experimentally infected piglets. In the period of investigation (DAI 2-10) there were two stages of the development of the density of the enzyme reaction product. The first stage can be characterized by an increase, the other by a decrease in the level of acid phosphatase activity. Enterocytes are influenced in both stages, but the decrease in the density of the reaction product of acid phosphatase was observed only in absorption cells, and not in goblet cells. The increase in the activity of acid phosphatase occurs in the periods of DAI 4 and 9-10. Enzymatic deviations occur mainly in the absorption cells of the mucosa of duodenum and middle jejunum; in the cells of posterior jejunum and ileum an increase in the density of the reaction product of acid phosphatase was also demonstrated, but at the lower quantitative level (especially on DAI 4). The decrease in the activity of acid phosphatase has a protracted development and it takes place on DAI 5 to 8.(ABSTRACT TRUNCATED AT 400 WORDS)     

The activity and properties of adenosine triphosphatase in various swine organs (liver, cerebral and kidney cortex, small intestinal mucosa)]

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.     

Immunological investigation of intestinal, liver, kidney, bone, placental and serum alkaline phosphatase in cattle

The purpose of this study is to investigate the immunological difference between intestinal, liver, kidney, bone, placental and serum alkaline phosphatase (ALPs) in cattle. Kidney, bone and placental ALPs were purified from each tissue by gel filtration and ion-exchange chromatographies, and intestinal, liver, and placental ALPs were obtained from a commercial source. The antibody to each tissue ALP was prepared by immunizing rabbits and tested by double immunodiffusion analysis in cross reactivities. The results indicated that the bovine tissue ALPs are divided into four groups in antigenicity, that is, intestinal, bone, liver and kidney-placental ALPs. The fetus, calf and cow sera contained bone ALP, and calf and cow sera also contained kidney or placental ALP, but all of the sera did not contain intestinal and liver ALP.     

Studies on the properties of acid erythrocyte phosphatase in sheep and the isoenzymes of sheep and goat acid erythrocyte phosphatase]

Ovine erythrocytic acid phosphatase showed two peaks of activity at pH 5.0 and 5.7 in acetate buffer with p-nitrophenylphosphate as substrate. The enzyme was only slightly inhibited by fluoride and L-phenylalanine, but high concentrations of urea strongly inhibited it. Activity of the enzyme was greater in goat erythrocytes than in sheep. By means of starch electrophoresis, three isoenzymes belonging to nine types were separated from the ovine enzymes, while three isoenzymes of five types were present in goats. Electrophoresis in polyacrylamide gel was suitable for detecting the rapidly migrating isoenzymes.     

Enzyme arrangement of various tissues in swine. 3. Studies of pre- and postnatal activities of various enzymes (ATPase, GOT, GPT, leucine aminopeptidase, acid and alkaline phosphatases, aldose reductase, glucuronate reductase, sorbitol dehydrogenase) in various tissues]

The crude protein levels as well as the activities of various enzymes were studied in certain tissues of fetuses (80th through 114th days of development), piglets of different age groups, and pigs for slaughter. In most of the tissues tested the postnatal activities of Na-K-ATPase were beyond those recorded from fetuses. The highest GOT activities were recorded from the liver, myocardium, and kidneys. Activities were found to rise sizeably in some tissues after birth. The activity of GPT, too, exhibited age-dependent variations. The activity of leucine-aminopeptidase increased strongly after birth in liver and kidneys. Acid phosphatase activity was less markedly influenced by development phases. Those enzymes which are involved in the formation of fructose and glucose (aldolreductase, glucuronate-reductase, and sorbite-dehydrogenase) had their highest activities, all age-dependent, in liver and kidneys.     

Obstruction of the small intestine by a trichobezoar in cattle: 15 cases (1992-2002)

OBJECTIVE: To determine historical and clinical findings, treatment, and outcome for cattle with small intestinal obstruction caused by a trichobezoar. DESIGN: Retrospective case series. ANIMALS: 15 cattle. PROCEDURES: Medical records of cattle with a diagnosis of small intestinal obstruction by a trichobezoar from 1992 to 2002 were reviewed. Information pertaining to various aspects of diagnosis, treatment, and outcome was collected from records. RESULTS: Trichobezoars were more common in young cattle, and affected cattle did not deteriorate clinically as rapidly as cattle with other types of intestinal obstruction. The most common initial owner complaints included decreased or absent fecal output, inappetance, abdominal distension, and signs of abdominal pain. Common clinical findings were dehydration, decreased or absent rumen motility, signs of depression, splashing sounds during succussion of the abdomen, and a pinging sound on percussion of the abdomen. The jejunum was obstructed in 10 cattle. Hypochloremic metabolic alkalosis and chronic inflammation were common laboratory findings. All 4 cattle that underwent abdominocentesis had peritonitis. The obstructing trichobezoar was removed surgically in 9 cattle, of which 7 survived and 2 died. The 6 cattle treated medically died or were euthanized. CONCLUSIONS AND CLINICAL RELEVANCE: Obstruction of the small intestine by a trichobezoar is uncommon, but it should be considered as a differential diagnosis in cattle with signs of intestinal obstruction, particularly if they are younger than 4 years of age and have a history of nonacute signs of intestinal obstruction. Surgical removal appears to be a favorable method of treatment and should be considered when this condition is suspected.     

Nitrogen and amino acid resorption in the small intestine of growing swine. 1. Animal study method, nitrogen content and amino acid composition of the small intestine chyme by administration of various proteins

The amount of endogenous N in the chyme at the end of the small intestine and the amino acid composition of the ileum chyme were ascertained with growing pigs with ileorectostomy after feeding qualitatively differentiated protein sources. In dependence on the protein used, distinct differences turned out for some amino acids with regard to their content in the ileum chyme. Bacteriologic and histologic investigations subsequent to the dissection of the test animals showed that - in comparison to the control animals-the functions of the small intestine remained the same during the time of the experiment. The experiment method described appears to be suitable for absorption investigations up to the end of the small intestine of growing pigs.