Analyze Diet

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.
Plasma bile acid elevation following CCI4 induced liver damage in dogs, sheep, calves and ponies.
Research in veterinary science    March 1, 1976   Volume 20, Issue 2 127-130 
Anwer MS, Engelking LR, Gronwall R, Klentz RD.Plasma bile acid concentration was determined in normal dogs,sheep, calves and ponies for three days before and six days after liver damage, induced by carbon tetrachloride. In all species, a significant increase in plasma bile acid concentration was associated with a concomitant significant increase in plasma sorbitol dehydrogenase and transferase activity. Plasma bilirubin also significantly increased in all animals except the dogs. Results suggested that plasma bile acid levels could be used to test liver function in domestic animals.
Evaluation of adenosine deaminase and other purine salvage pathway enzymes in horses with combined immunodeficiency.
Infection and immunity    March 1, 1976   Volume 13, Issue 3 995-997 doi: 10.1128/iai.13.3.995-997.1976
McGuire TC, Pollara B, Moore JJ, Poppie MJ.Foals with combined immunodeficiency had normal levels of purine salvage pathway enzymes, including adenosine deaminase, nucleoside phosphorylase, and xanthine oxidase.
The effect of exercise on the lactic dehydrogenase and creatine kinase isoenzyme composition of horse serum.
Research in veterinary science    March 1, 1976   Volume 20, Issue 2 191-196 
Anderson MG.The distribution of lactic dehydrogenase, aldolase and creatine kinase in various horse tissues was determined. Using polyacrylamide gel electrophoresis the lactic dehydrogenase and creatine kinase isoenzyme composition of horse serum, taken before and after exercise, was studied. Horse tissue isoenzyme patterns were also obtained. By comparing tissue and serum patterns, skeletal muscle was found to be the tissue of origin of the increase in serum lactic dehydrogenase and creatine kinase observed after exercise.
Studies on metabolism and effects of estrogen on pituitary prolactin and LH secretion.
Journal of toxicology and environmental health    March 1, 1976   Volume 1, Issue 4 641-655 doi: 10.1080/15287397609529363
Chen CL, Pattison ML, Engleking LR, Gronwall RR.The effect of a subcutaneous injection of estradiol on the secretion of pituitary prolactin in the rat and the relationship between serum estradiol level and luteinizing hormone (LH) secretion in mare were reviewed. In addition, the effect of estradiol injection on LH secretion and the metabolism of [14C] estradiol in intact and bile duct fistulated pony mares were studied. Low (0.1 mug/day/rat) to moderate dose (5 mug/day/rat) of estradiol benzoate injected subcutaneously to mature or immature rats significantly increased pituitary content of prolactin and serum prolactin level five- to tenfo...
Isolation and some molecular parameters of elastase-like normal proteinases from horse blood leucocytes.
The Biochemical journal    February 1, 1976   Volume 153, Issue 2 389-396 doi: 10.1042/bj1530389
Dubin A, Koj A, Chudzik J.Cytoplasmic granules were isolated from horse blood polymorphonuclear leucocytes by the heparin method and extracted with 0.9% NaCl by repeated freezing. Soluble proteins were separated on a column of Sephadex G-75 followed by chromatography on a column of CM-Sephadex with a NaCl gradient. Gel filtration, density-gradient centrifugation, isoelectric focusing and 0.1% sodium dodecyl sulphate/polyacrylamide-gel electrophoresis at pH 7.0 and at pH 4.5 were used to determine molecular parameters of proteinases. Three enzymes hydrolysing both casein and N-benzyloxycarbonyl-L-alanine nitrophenyl est...
Substrate specificity and modifications of the active centre of elastase-like neutral proteinases from horse blood leucocytes.
The Biochemical journal    February 1, 1976   Volume 153, Issue 2 397-402 doi: 10.1042/bj1530397
Koj A, Chudzik J, Dubin A.Two proteinases (2A and 2B) purified from the granular fraction of horse blood leucocytes degrade casein (Km values 12.8 and 6mg/ml respectively) with maximum activity at pH 7.4 and in the presence of 2m-urea. Urea-denatured haemoglobin, fibrinogen, albumin and resorcin/fuchsin-stained elastin are digested at a slower rate. The enzymes hydrolyse synthetic substrates of elastase, N-benzyloxycarbonyl-L-alanine 4-nitrophenyl ester (Km 0.114 and 0.178 mM) and N-acetyl-tri-L-alanine methyl ester (Km 5.55 and 0.98 mM), but they do not hydrolyse synthetic substrates of trypsin, chymotrypsin and throm...
Immunochemical studies on blood groups. Structures and immunochemical properties of nine oligosaccharides from B-active and non-B-active blood group substances of horse gastric mucosae.
Archives of biochemistry and biophysics    February 1, 1976   Volume 172, Issue 2 353 
Newman W, Kabat EA.No abstract available
Immunochemical studies on blood groups. Purification, chemical and immunochemical properties of blood group-active glycoproteins from horse gastric mucosae.
Archives of biochemistry and biophysics    February 1, 1976   Volume 172, Issue 2 510-523 doi: 10.1016/0003-9861(76)90104-1
Newman W, Kabat EA.No abstract available
Cell-free synthesis of equine herpesvirus type 3 nucleocapsid polypeptides.
Virology    February 1, 1976   Volume 69, Issue 2 751-762 doi: 10.1016/0042-6822(76)90503-1
Allen GP, Bryans JT.No abstract available
Immunochemical studies on blood groups. Immunochemical properties of B-active and non-B-active blood group substances from horse gastric mucosae and the relative size distributions of oligosaccharides liberated by base-borohydride.
Archives of biochemistry and biophysics    February 1, 1976   Volume 172, Issue 2 524-534 doi: 10.1016/0003-9861(76)90105-3
Newman W, Kabat EA.No abstract available
Concentration of prostaglandins F in uterine venous plasma of anesthetized mares during the estrous cycle and early pregnancy.
Prostaglandins    February 1, 1976   Volume 11, Issue 2 251-260 doi: 10.1016/0090-6980(76)90148-9
Douglas RH, Ginther OJ.Prostaglandins F were quantitated by radioimmunoassay in uterine venous plasma of anesthetized mares on day 7 of estrus, days 2, 6, 10, 14 or 18 of diestrus and days 10, 14 or 18 of pregnancy. The PGF concentration was greater (P less than .01) at day 14 of diestrus than at all other days studied. The concentrations at days 10 and 18 of diestrus and at days 10, 14 and 18 of pregnancy were greater (P less than .05) than at day 7 of estrus and days 2 and 6 of diestrus. PGF concentrations at days 10 and 14 were greater (P less than .01) for diestrous than for pregnant mares.
Fiber types and size in equine skeletal muscle.
American journal of veterinary research    February 1, 1976   Volume 37, Issue 2 145-148 
Aberle ED, Judge MD, Kirkham WW, Page EH, Crawford BH.Frozen sections of equine musculus semitendinosus were examined for myosin adenosine triphosphatase (ATPase) and reduced nicotinamide adenine dinucleotide-tetrazolium reductase (NADH-TR), using standard histochemical procedures, and the proportions of the various fiber types and average fiber sectional size were determined. With ATPase staining, approximately 70% of the fibers were classified as alpha fibers (ATPase positive), and 30%, as beta fibers (ATPase negative). In addition, 2 populations of alpha fibers could be readily distinguished on the basis of the intensity of the ATPase reaction...
Primary structure determination of two cytochromes c2: close similarity to functionally unrelated mitochondrial cytochrome C.
Proceedings of the National Academy of Sciences of the United States of America    February 1, 1976   Volume 73, Issue 2 472-475 doi: 10.1073/pnas.73.2.472
Ambler RP, Meyer TE, Kamen MD.The amino-acid sequences of the cytochromes c2 from the photosynthetic non-sulfur purple bacteria Rhodomicrobium vannielii and Rhodopseudomonas viridis have been determined. Only a single residue deletion (at position 11 in horse cytochrome c) is necessary to align the sequences with those of mitochondrial cytochromes c. The overall sequence similarity between these cytochromes c2 and mitochondrial cytochromes c is closer than that between mitochondrial cytochromes c and the other cytochromes c2 of known sequence, and in the latter multiple insertions and deletions must be postulated before a ...
Oxidation of human and animal haemoglobins with ascorbate, acetylphenylhydrazine, nitrite, and hydrogen peroxide.
British journal of haematology    February 1, 1976   Volume 32, Issue 2 193-203 doi: 10.1111/j.1365-2141.1976.tb00922.x
Harvey JW, Kaneko JJ.Partially purified haemoglobin solutions of man, horse, car and dog were oxidized with ascorbate, acetylphenylhydrazine, nitrite, and H2O2 at 25 degrees C and with ascorbate and acetylphenylhydrazine at 37 degrees C. Haemoglobins of the carnivores were more easily oxidized with ascorbate, nitrite, and H2O2 than equine and human haemoglobins. Feline haemoglobin, in general, appeared more susceptible to oxidation, particularly oxidative denaturation, than those of the other species. In addition, results of the incubations at 37 degrees C suggest that feline haemoglobin B might be more susceptibl...
Characterization of human, bovine, and horse antithrombin III.
Biochemistry    January 27, 1976   Volume 15, Issue 2 368-373 doi: 10.1021/bi00647a020
Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW.A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single poly...
Chemical modification as a probe of the topography and reactivity of horse-spleen apoferritin.
European journal of biochemistry    January 15, 1976   Volume 61, Issue 2 545-550 doi: 10.1111/j.1432-1033.1976.tb10049.x
Wetz K, Crichton RR.In apoferritin, but not in ferritin, 1.0 +/- 0.1 cysteine residue per subunit can be modified. In ferritin 3.3 +/- 0.3 lysine residues and 7.1 +/- 0.7 carboxyl groups per subunit can be modified, whilst the corresponding values for apoferritin are 4.4 +/- 0.4 lysine residues and 11.0 +/- 0.4 carboxyl groups per subunit. Modification of lysine residues which maleic anhydride and carboxyl groups with glycineamide in apoferritin which has been dissociated and denatured in guanidine hydrochloride leads to the introduction of 9.1 +/- 0.5 maleyl groups per subunit and 22.0 +/- 0.9 glycineamide resid...
Ligand binding properties of horse hemoglobins containing deutero- and mesoheme.
The Journal of biological chemistry    January 10, 1976   Volume 251, Issue 1 45-52 
Seybert DW, Moffat K, Gibson QH.The reactions of horse globin reconstituted with proto-, deutero-, and mesoheme have been examined by equilibrium and kinetic methods. In virtually all reactions studied, mesohemoglobin displays the more extreme functional behavior, whereas deuterohemoglobin exhibits behavior which is either very similar to native hemoglobin or intermediate between the two. Our kinetic and equilibrium results indicate that the primary effect of heme modification on the functional properties of hemoglobin is to alter the intrinsic reactivities of the deoxy and liganded conformations. Heme modification does not,...
Variation of some blood biochemical characteristics in cattle, horses and dogs, and causes of such variations.
Annales de recherches veterinaires. Annals of veterinary research    January 1, 1976   Volume 7, Issue 2 125-128 
Ekman L.No abstract available
[Values of acid-base equilibrium in the blood of various species of domestic animals].
Veterinarni medicina    January 1, 1976   Volume 21, Issue 1 51-59 
Komárek J, Stros K, Sýkora I, Kynclová I, Jadrný L, Selinger P.By means of the Astrup equilibration method the values of the acid-base balance of the blood were determined in 104 cows, 99 horses, 100 pigs, 15 sheep, 20 goats, and in 101 dogs. The pH values of the blood, the partial pressure of CO2, the base excess, the base buffer, the standard bicarbonate, the actual bicarbonate, and the total CO2 were processed statistically and are presented in tables.
Purification, characterization, and quantitation of the antigen employed in the immunodiffusion test for diagnosis of equine infectious anemia.
Preparative biochemistry    January 1, 1976   Volume 6, Issue 2-3 193-211 doi: 10.1080/00327487608061612
Hart LT, Braymer HD, Larson AD, Broussard EA.Equine infectious anemia (EIA) antigen extracted from the spleen of horses infected with EIA virus was purified by pH treatment, (NH4)2SO4 fractionation and affinity chromatography. The homogeneity of the antigen was indicated by sedimentation rate and sedimentation equilibrium experiments. A S20,w of 0.51 was determined and a molecular weight of 7600 was calculated from sedimentation equilibrium analysis. The amino acid composition of the pure antigen indicated the antigen is an acidic protein. Employing radical immunodiffusion (RID) and pure antigen a method for quantitating antigen content ...
[Equine pepsins].
Biokhimiia (Moscow, Russia)    January 1, 1976   Volume 41, Issue 7 1285-1290 
Stepanov VM, Lavrenova GI, Rudenskaia GN, Gonchar MV, Lebareva LS.6 forms of pepsin are found in horse gastric juice. Amino acid sequence is determined of N-terminal (most variable) part of polypeptide chain of main pepsin components. Equine pepsines, which have pI 2.1 and 2.3, are found to have identical amino acid sequence at least for 31 amino acid residues. The same sequence is observed in the component with pI 2.6 for 10 first residues. The sequence of equine pepsin with pI 3.2 has 3 substitutions for 33 amino acids, when compared with pepsines having pI 2.1 and 2.3. The forms of equine pepsin studied are more similar than the other isoenzyme pair, huma...
Comparative studies of human, equine, porcine and bovine erythrocyte membrane sialoglycoproteins.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1976   Volume 55, Issue 1 37-44 doi: 10.1016/0305-0491(76)90169-3
Hamazaki H, Hotta K, Konishi K.No abstract available
Isolation and partial characterization of three major allergens of horse hair and dandruff.
International archives of allergy and applied immunology    January 1, 1976   Volume 51, Issue 1 48-67 doi: 10.1159/000231578
Løowenstein H, Markussen B, Weeke B.Three major allergens of horse hair and dandruff have been isolated. The fractionation procedures involved various combinations, described in detail, of ethanol precipitation below --5degreesC, cation- and anion-exchange chromatography, and gel filtration. UV absorption, quantitative immunoelectrophoresis and RAST inhibition were used to monitor the separations. Protein impurities constituted less than 5% in all cases. The molecular weights of the isolated proteins were 1.9 X 10(4), 5.1 X 10(4) and 3.1 X 10(4) daltons, respectively. The pIs were determined as 4.1, 3.8 and 3.9, respectively. Th...
Acid phosphatase heterogeneity in horse neutrophil and eosinophil leukocytes.
Enzyme    January 1, 1976   Volume 21, Issue 6 540-552 doi: 10.1159/000458906
Heyneman RA, Bruyninckx WJ, Vercauteren RE.Two distinct groups of acid phosphatase containing granules were characterized in neutrophils, each group displaying different multiple forms of the enzyme. The heavy granule acid phosphatase showed a lysosomal location. A second lighter group of particles contained a thermolabile, thiol-dependent acid p-nitrophenyl and alpha-naphtylphosphatase, an enzyme clearly different from lysosomal acid phosphatase. Acid phosphatase activity from eosinophil leukocytes appeared to be totally associated with the typical eosinophil granules. On mechanical disruption of these particles, an acid phosphatase w...
Nutrition and bone development in horses.
Journal of the American Veterinary Medical Association    January 1, 1976   Volume 168, Issue 1 39-44 
Hintz HF, Schryver HF.No abstract available
[Comparison of free amino acids in human and animal blood serum. III. Man, cat, cattle and horse].
Zeitschrift fur Tierphysiologie, Tierernahrung und Futtermittelkunde    January 1, 1976   Volume 36, Issue 3 170-174 
Anda LP, Liappis N.No abstract available
Creatine phosphokinase in normal sheep and in sheep with nutritional muscular dystrophy.
Journal of comparative pathology    January 1, 1976   Volume 86, Issue 1 23-28 doi: 10.1016/0021-9975(76)90023-2
Boyd JW.No abstract available
Primary structure of equine growth hormone.
International journal of peptide and protein research    January 1, 1976   Volume 8, Issue 5 435-444 doi: 10.1111/j.1399-3011.1976.tb02523.x
Zakin MM, Poskus E, Langton AA, Ferrara P, Santomé JA, Dellacha JM, Paladini AC.No abstract available
LDH and LDH isoenzymes of synovial fluid in the horse.
Acta veterinaria Scandinavica    January 1, 1976   Volume 17, Issue 2 178-189 doi: 10.1186/BF03547926
Rejnö S.LDH is an intracellular enzyme, which when cells degenerate is released to the extracellular spaces and body fluids. Cells and organs in the mammalian body differ from each other with respect to their LDH isoenzyme patterns. These circumstances have led to the use of LDH isoenzyme determinations in laboratory diagnostic work. In the present investigation total LDH activity and LDH isoenzyme distribution in equine synovial fluid from healthy joints, joints with serous arthritis, osteochondrosis dissecans and arthrosis, were determined. The fluids from the diseased joints differed from normal sy...
Muscle structure and function–an explanation.
Equine veterinary journal    January 1, 1976   Volume 8, Issue 1 17-19 doi: 10.1111/j.2042-3306.1976.tb03276.x
Stewart M.The structure of vertebrate skeletal muscle is reviewed. The mechanism of muscular contraction and its control is then discussed from the point of view of molecular structure. Contraction takes place by a sliding filament mechanism produced by cross-bridges which form between thick and thin filaments. Control is exercised by tropomyosin and troponin. When the calcium concentration is low, these proteins interfere with the formation of cross-bridges and prevent contraction, but when the calcium concentration is increased, they no longer interfere and contraction proceeds.