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Topic:Biochemistry
The study of biochemistry in horses encompasses the chemical processes and substances that occur within equine organisms. This field investigates the molecular interactions and pathways that are fundamental to horse physiology, including metabolism, enzyme activity, and genetic expression. Key areas of interest include the examination of metabolic disorders, nutrient absorption, and the biochemical basis of muscle function and energy production. Researchers utilize biochemical analysis to understand health and disease mechanisms in horses, contributing to the development of diagnostic tools and therapeutic strategies. This page gathers peer-reviewed studies and scholarly articles that explore various biochemical processes and their implications for equine health and performance.
Carboxylesterases (EC 3.1.1). Purification and titration of chicken, sheep, and horse liver carboxylesterases. Chicken, sheep, and horse liver carboxylesterases have been purified by procedures involving ammonium sulfate fractionation, ion-exchange chromatography and gel filtration on Sephadex. The actual yields of the procedures described were as follows: chicken, 1 g from 2 kg of liver powder (chloroform-acetone); sheep, 200 mg from 400 g of powder (chloroform-acetone); horse, 230 mg from 800 g of powder (acetone). The purified enzymes are free of non-carboxyl-esterase protein as shown by gel electrophoresis, although they do contain electrophoretic variants. The equivalent weight of the chicken enzy...
Formation of steroids by the pregnant mare. V. Metabolism of 14C-isopentenylpyrophosphate and 3H-dehydroisoandrosterone injected into the fetus. A mixture of 1-14C-isopentenylpyrophosphate and 3H-dehydroisoandrosterone was injected into a horse fetus intramuscularly during laparotomy, after which maternal urine was collected for 4 days. Steroid conjugates in the urine were extracted with Amberlite XAD-2 resin, hydrolysed and separated into phenolic and neutral fractions. From the phenolic fraction estrone, 17alpha-estradiol, equilin and equilenin were isolated. Only estrone and 17alpha-estradiol contained both 3H and 14C, while the ring B unsaturated estrogens contained only 14C. From the neutral fraction 14C-labeled 3beta-hydroxy-5alp...
Intestinal obstruction in the horse. Physical signs and blood chemistry. Physical signs and blood changes were studied in horses with artificially produced obstructions of the duodenum and the small colon and simulated volvulus of the ileum. Horses with obstruction of the duodenum had the most violent physical signs and the shortest survival time. Blood changes were an initial rise in pH followed by acidosis, hyperkalemia and a decrease in HCO3 minus, Na+ and C1 minus. Obstruction of the small colon resulted in mild physical signs. The blood parameters recorded were normal. Simulated volvulus resulted in continuous colic. Blood changes were acidosis and hyperkalemi...
[Relationship of citric acid concentration to various quality indices of the equine ejaculate]. The paper describes the relation of citric acid to other chemical and biological indices of the fertility of stallion sperm. A positive relation was found between citric acid and the density and motility of spermatozoa, to the concentration of ergothioneine, and hemolytic activity, and a negative relation to pH and to the polarographic activity of proteins. Attention is drawn to the important nutritional function of citric acid.
An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase. The kinetics of the horse liver alcohol dehydrogenase (alcohol: NAD+ oxidoreductase EC 1.1.1.1) catalyzed metabolism of octanol and octanal to octanoic acid have been examined. On incubation of octanol with horse liver alcohol dehydrogenase in the presence of NAD+, NADH as well as octanal and octanoic acid were seen as the initial products. However, on continued incubation, the octanal concentration progressively decreased to where only negligible quantities were present in the incubation after 10 min. The production of NADH was biphasic. An initial phase was followed in about 2 min with a slo...
Species variability in the modification of erythrocyte surface proteins by enzymatic probes. Bovine and equine erythrocytes have been studied by three different surface modification techniques to investigate the accessibility of the surface components to the external medium. Lactoperoxidase labeling of equine erythrocytes results in a significant labeling of only one membrane component, a 100 000-mol.wt polypeptide corresponding to the membrane-spanning Component III of human erythrocytes. The major sialoglycoprotein of the equine erythrocyte is not labeled. This is in contradistinction to the situation for human and bovine cells, where both components are labeled. The equine membrane...
[Sterols of horse erythrocytes]. Sterols of the whole erythrocytes, hemoglobin, membranes and their protein fractions were studied. Erythrocytes and their components were established to contain, besides cholesterol, other substances of the sterol nature. Cholesterol, 7-dehydrocholesterol and other substances of the cholesterol series are practically completely linked with the lipoproteid fractions of the erythrocyte membrane whereas all sterols found in the native erythrocytes in negligible amounts are bound with hemoglobin.
Mercuri-nitrophenol as a reporter group for the conformational change of hemoglobin. One mole of horse hemoglobin tetramer reacts with 2 moles of 2-chloromercuri-4-nitrophenol (MNP) at beta 93 cysteine. The difference spectra between NMP-bound hemoglobin and hemoglobin, measured with the aid of ascorbic acid and ascorate oxidase [EC 1.10.3.3] as deoxygenation reagents, indicate that the pK of the phenolic hydroxyl group of MNP increases by 0.6 to 0.8 pH unit on deoxygenation of the hemoglobin. The Hill constant of the modified hemoglobin changes with pH. It decreases from about 2.4 at pH 6.8 to about 1.0 at pH 9.0 This effect of the reagent is interpreted as inherent to the re...
Carbohydrate digestion and absorption in the equine small intestine. Dietary carbohydrates, which constitute a most important source of equine nutrition, are digested and absorbed by a series of complex processes principally in the small intestine, beginning with intraluminal starch hydrolysis by the action of pancreatic amylase. The continuous secretion of a copious volume of pancreatic juice, low in enzyme activity, presumably releases sufficient oligosaccharides for further hydrolysis at the intestinal cell surface by brush border enzymes. Active carrier mediated mechanisms then transport the final hexose products across the intestinal cell for uptake in the...
Comparative analyses of members of the Venezuelan equine encephalomyelitis virus complex. Polyacrylamide gel electrophoretic examination of viruses selected from the Venezuelan equine encephalomyelitis (VEE) complex revealed distinct strain to strain differences in profiles of the two virion envelope proteins. The core protein was identical in all viruses tested. We detected five electrophoretic patterns into which the virus strains could be classified and these were designated alpha (alpha), beta (beta), gamma (gamma), delta (delta), and episolon (episolon). Isolates representing variant E of subtype I exhibited a profile characterized by only one apparent envelope band. The epizo...
Certain physiochemical properties of uterine tubal fluid, follicular fluid, and blood plasma in the mare. Uterine tubal fluids were collected twice a day from mares for 5 consecutive estrous cycles between March 15 and September 1. Follicular fluids were aspirated from the follicles of exteriorized ovaries of 3 mares between days 2 and 5 of estrus. Uterine tubal fluid and follicular fluid were analyzed for osmolarity, dry matter, total lipids, total free fatty acids, glucose, fructose, and lactic acid. Blood samples were collected (jugular venipuncture) throughout the estrous cycle, and the same physical and biochemical analyses were made on blood plasma. A difference (P less than 0.01) was found ...
Identification of the lysine residue modified during the activation of acetimidylation of horse liver alcohol dehydrogenase. A single amino group in horse liver alcohol dehydrogenase was modified with methyl(14C)acetimidate by a differential labeling procedure. Lysine residues outside the active site were modified with ethyl acetimidate while a lysine residue in the active site was protected by the formation of an enzyme-NAD+-pyrazole complex. After the protecting reagents were removed, the enzyme was treated with methyl(14C)acetimidate. Enzyme activity was enhanced 13-fold as 1.1 (14C)acetimidyl group was incorporated per active site. A labeled peptide was isolated from a tryptic-chymotryptic digest of the modified...
Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study. The binding of Au(CN)2- and Pt(CN)4-2- ions to the coenzyme binding site of horse liver alcohol dehydrogenase (alcohol : NAD+ oxidoreductase EC 1.1.1.1) has been studied by 35C1 nuclear magnetic relaxation. Longitudinal relaxation rates were analyzed in terms of a simple model and binding constants for Au(CN)2-, Pt(CN)4-2- and C1- were estimated. From a comparison between transverse and longitudinal relaxation rates the correlation time and the quadrupole coupling constant of bound chloride ion were obtained. The quadrupole coupling constant estimated from a simple electrostatic model for chlo...
Conformational studies of equilibrium structures in fragments of horse heart cytochrome c. Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
[Comparative study of the optimum pH value of serum alkaline phosphatase in various species of farm animals]. Investigations were carried out on the alkaline phosphatase in the sera of cattle, horses, pigs, sheep, goats, and chickens, the pH value of the buffer used being 9.0-9.8-10.0-10.2-10.6 and 11.0, and the method applied--that of Richterich. The pH value at which the serum alkaline phosphatase in the various farm animals and birds was most active was found to vary to a large extent. Optimal values for the enzyme's activity usually range as follows: cattle, 10.2; pigs and goats, 10.0; sheep,--10.2; horses,--9.8; chickens,--10.6.
