Topic:Enzymes
Enzymes are biological catalysts that facilitate biochemical reactions in horses by lowering the activation energy required for these processes. They are involved in various physiological functions, including digestion, metabolism, and cellular repair. Common enzymes in equine biology include amylase, lipase, and lactate dehydrogenase, each playing a specific role in the breakdown of nutrients and energy production. The activity and concentration of these enzymes can vary in response to different physiological and pathological conditions, serving as potential indicators in veterinary diagnostics. This page compiles peer-reviewed research studies and scholarly articles that explore the function, regulation, and clinical implications of enzymes in equine health.
Studies related to the metabolism of anabolic steroids in the horse: the identification of some 16-oxygenated metabolites of 19-nortestosterone. 1. The metabolism of 19-nor[4-14C]testosterone in a thoroughbred horse has been studied and neutral urinary metabolites obtained after enzyme hydrolysis have been investigated by g.l.c.-mass spectrometry. 2. 3-Hydroxyestran-17-one, 17 alpha- and 17 beta-nortestosterone, estrane-3,17-diol (two isomers), 3,16-dihydroxyestran-17-one (two isomers), 3,17-dihydroxyestran-16-one (two isomers) and estrane-3,16,17-triol were identified in the neutral urinary extracts.
Biochemical characterization of equine herpesvirus type 3-induced deoxythymidine kinase purified from lytically infected horse embryo dermal fibroblasts. Infection of horse KyED cells with equine herpesvirus type 3 (EHV-3) resulted in a sevenfold increase in cytosol deoxythymidine kinase (dTK) activity. The EHV-3 dTK was purified from KyED cytosol dTK by affinity chromatography on deoxythymidine-Sepharose and characterized with respect to its electrophoretic mobility, molecular weight, substrate specificity, phosphate donor specificity, and immunological specificity. The purified EHV-3 dTK migrated in polyacrylamide gels with an Rf of 0.30 and sedimented in glycerol gradients with an S value of 5.13, corresponding to a molecular weight of 83,00...
Biochemical effects of succinylcholine chloride in mechanically ventilated horses anesthetized with halothane in oxygen. Succinylcholine chloride administered to horses anesthetized with halothane in oxygen and mechanically ventilated, caused slight but statistically insignificant (P less than 0.01) increases in creatine phosphokinase, lactic dehydrogenase, and aspartate aminotransferase activity. The increases in these enzymes have been explained on the basis of muscle damage resulting from succinylcholine chloride induced muscle fasciculations and by hypoperfusion of tissues due to depression of the cardiovascular system caused by general anesthesia. These changes were not clinically apparent based upon the ab...
The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species. The effect of trypsin digestion on iron-saturated and iron-free (apo) human, rabbit, bovine, pig and horse tranferrins has been studied. Iron-binding fragments were produced only from iron-saturated pig and bovine transferrins although some cleavage of the polypeptide chain occurred in all cases. The apo-transferrins were generally degraded to a greater extent than the corresponding iron-saturated proteins. The ability of the different transferrins to donate iron to rabbit reticulocytes varied in the order rabbit approximately pig greater than human approximately horse greater than bovine. Try...
Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c. Spectrophotometric titrations of five singly modified horse heart ferricytochromes c, specifically (trifluoromethyl)phenylcarbamylated (CF3PhNHCO-) or trifluoroacetylated (CF3CO-) at lysines-13, -72, and -79, were carried out. The CF3PhNHCO-Lys-13, Lys-79, and CF3CO-Lys-79 derivatives all underwent alkaline isomerization with loss of the 695-nm band to low-spin species with an apparent pK of about 8.9, as did the unmodified cytochrome. However, modification of lysine-72 appeared to alter the reaction pathway since the CF3PhNHCO-Lys-72 derivative isomerized to a high-spin form with an apparent ...
Purification by affinity chromatography and characterization of a neutral alpha-glucosidase from horse kidney. A horse kidney neutral alpha-D-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) was purified about 580-fold with a yield of 33% by an affinity chromatography technique using the p-aminophenyl-beta-D-maltoside, a substrate derivative, as ligand. The purified enzyme, homogeneous in polyacrylamide gel electrophoresis, was a glycoprotein with a molecular weight of 280 000 as calculated by gel filtration and its isoelectric focusing points was found to be pH 4.1. The purified enzyme was able to hydrolyze various substrates having (alpha-1,2), (alpha-1,3), (alpha-1,4), and (alpha-1,6) glu...
Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism. It is known that His-48 is part of the active center in pancreatic phospholipase. To further elucidate the role of histidine-48 in the active center of pancreatic phospholipase A2, we have modified the enzyme with a number of bromo ketones and methyl benzenesulfonates. Rapid methylation occurred with methyl p-nitrobenzenesulfonate. Methylated phospholipase shows total loss of enzymatic activity whereas binding of substrate and the cofactor Ca2+ remains intact. Amino acid analysis of methylated equine phospholipase showed the loss of the single molecule of histidine and the formation of one mol...
A new method for the isolation of aminoacylase from mammalian kidneys. Aminoacylase (E.C. 3.5.1.14) was isolated from the kidneys of different mammalian species (horse, cattle, rabbit and pig) by extracting the organ with water and subjecting the extract to heat treatment at 70 degrees C for 10 min, then, after having removed denatured proteins by fractionating those remaining in the solution by ammonium sulfate. The enzyme obtained in this way can either be used directly for practical purposes (e.g. preparation of immobilized aminoacylase) or further purified by chromatography. For the further purification of porcine kidney aminoacylase we applied a combination ...
[Bacteriological studies of Haemophilus equigenitalis Taylor 1978, the causative organism of contagious equine metritis 1977 (author’s transl)]. The cultural, biochemical, antigenic and antibiotic susceptibility characteristics of 17 strains of Haemophilus equigenitalis, the causative organism of contagious equine metritis (CEM), were studied. Biochemical characteristics were investigated using both conventional method and the API ZYM system of enzyme detection. The biochemical profile of the H. equigenitalis strains was unique and differed from the other bacterial species studied under the same experimental conditions (H. influenzae and H. parainfluenzae, B. abortus and B. melitensis, P. multocida, A. calcoaceticus). The required X an...
Serum alkaline phosphatase in pregnant mares. Serum alkaline phosphatase was measured in ten mares during various stages of gestation. No significant change in serum alkaline phosphatase activity was detected during pregnancy. These data suggest that interpretation of serum alkaline phosphatase in horses can be made independently of their pregnancy status.
Metabolism of progesterone by placentas from several mammalian species in vitro. 20-alpha-Hydroxysteroid oxidoreductase (20-alpha-HSDH) activity and 20-alpha-dihydroprogesterone concentration (20-alpha-DHP) reach peak values in the human placenta after vaginal delivery. To determine if these findings are unique to the human, we measured 20-alpha-HSDH activity as well as endogenous progesterone (P) and 20-alpha-DHP concentration in the soluble supernatant fraction of placental tissues obtained from rodents (rat, rabbit, guinea pig), ungulates (horse, zebra, giraffe, cow), and primates (squirrel monkey, orangutan, man). P concentration was very low in rodents (mean 0.60 ng/m...
Isoenzymes of equine alkaline phosphatase. Alkaline phosphatase isoenzymes from small intestine, cecum, large colon, small colon, liver, kidney, leukocytes, and serum from ten clinically normal horses were defined by their sensitivities to L-phenylalanine, L-homoarginine, levamisole and heat, and by polyacrylamide gel disc electrophoresis. Readily identifiable isoenzymes occurred in small intestine, granulocytes, kidney, cecum, and large and small colon. By contrast, alkaline phosphatases from liver, lymphocytes, and serum could not be discriminated by this group of tests.
Plasma and synovial fluid lysozyme activity in horses with experimental cartilage defects. Cartilaginous defects were created in the radiocarpal joints of 12 horses. Synovial fluid cytologic features, lysozyme activity, and beta-glucuronidase activity were monitored for 16 days. A comparison was made of plasma lysozyme and beta-glucuronidase activity and of synovial fluid lysozyme, beta-glucuronidase, and leukocyte concentrations. Plasma lysozyme was found to be independent of synovial fluid lysozyme activity. Synovial fluid lysozyme was significantly increased (P less than 0.001) in all joints with surgically induced defects (group I) compared with controls (arthrocentesis done; gr...
Differences in the interactions of liver alcohol dehydrogenases with probes binding into the substrate pocket. The interactions of three groups of probes (berberine alkaloids, tricyclic psychopharmaca and acridine derivatives) with isoenzymes of horse liver alcohol dehydrogenase and with rat liver alcohol dehydrogenase have been examined. These compounds inhibit the activity of the EE isoenzyme of horse liver alcohol dehydrogenase but differ in their behaviour towards the steroid-active enzymes (i.e. the ES isoenzyme of horse liver alcohol dehydrognase and alcohol dehydrogenase from rat liver): psychopharmaca inhibit, acridines activate and berberines do not bind. The ligands differ also in their influ...
Tissue and plasma activity of lactic dehydrogenase and creatine kinase in the horse. Lactic dehydrogenase, although widely distributed in most tissues, was more highly concentrated in skeletal muscle, cardiac muscle, kidney and liver. Isoenzyme patterns showed a selective concentration of LDH5 in skeletal muscle while in the heart LDH 1 and 2 were predominant. In contrast, creatine kinase was only present in substantial concentration in skeletal and cardiac muscle. The serum concentrationof both enzymes showed a wide range of activity.
Colic in the horse. A clinical and clinical chemical study of 42 cases. 42 horses were examined. The physical signs with relation to circulatory insufficiency and the abdominal disease were registered following a two-phased examination procedure. Great prognostic value was found in the degree of circulatory insufficiency judged by pulse rate and character, filling of the jugular vein, skin temperature, colour of mucous membranes, capillary refill time, sweating, depression, skin turgor and degree of enophthalmus. In making a causal diagnosis the abdomen was examined for shape, tenderness, peristaltic sounds, gastric dilation by siphoning, abnormal rectal findings ...
Oxidation of (horse) hemoglobin by copper: an intermediate detected by electron spin resonance. The oxidation of horse hemoglobin by Cu(II) has been followed by the changes in the electron spin resonance spectra of copper. By stopped-flow and freeze-quenching techniques, it is shown that the second-order rate constant for the binding of Cu(II) to hemoglobin is greater than 5 X 10(5) mol-1 s-1 and the apparent first-order rate for the reduction of Cu(II) to Cu(I) is 0.051 s-1. It is also shown that the binding of Cu(II) to hemoglobin is followed by an alteration of the Cu(II) spectrum, decreasing the g values. This process has an apparent rate constant of 17 s-1 and presumably involves a ...
Purification of the subunit Clq from the first component of equine complement. Initial separation and concentration of Clq from fresh, normal equine serum was accomplished by precipitation in 0.02 M acetate buffer, pH 5.5, at 4 degrees for 24 h. The re-dissolved precipitate was clarified by centrifugation at 80,000 g for 1 h and then dialysed against Tris-HCl buffer (0.05 M, pH 8.0) containing 10-3 M EDTA. The clarified dialysate remained biologically active at 5 degrees for at least 4 weeks. Biological activity of equine Clq was determined by assay of its ability to agglutinate sensitized sheep erythrocytes (EA). Following ammonium sulphate fractionation, Sepharose 4B g...
Studies related to the metabolism of anabolic steroids in the horse: testosterone. 1. After intramuscular administration of [4-14C]testosterone to two cross-bred gelded horses, 45% of the radioactivity was excreted in urine in 96 h. Small amounts of urinary activity could still be detected at 200 h. 2. Neutral metabolites obtained after both enzyme and acid hydrolysis of urine samples have been investigated by g.l.c.-mass spectrometry. 3. 5 alpha-Androstane-3 beta, 17 alpha-diol was found only in the enzyme-hydrolysable extract and testosterone only in the acid-hydrolysable extract. 5 alpha-Androstane-3 beta, 17 beta-diol and 3 beta-hydroxy-5 alpha-androstan-17-one were foun...
Seasonal relationship between pineal hydroxyindole-O-methyltransferase (HIOMT) activity and reproductive status in the pony. Pony pineal glands and female reproductive tracts were collected monthly for 1 year from
a local slaughterhouse. Pineal gland weights did not change significantly throughout the year.
Pineal gland tissue homogenates were assayed for hydroxyindole-O-methyltransferase
(HIOMT) activity with N-acetylserotonin as the primary substrate. The greatest HIOMT
activity was obtained with N-acetylserotonin as substrate. but three other related S-OH
indole substrates (5-hydroxytryptophol, serotonin. and 5-hydroxy-2-methylindole) were also
methylated. HIOMT activity with all substrates was highest duri...