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.
Sweat gland function in isolated perfused skin.
The Journal of physiology    September 1, 1975   Volume 250, Issue 3 633-649 doi: 10.1113/jphysiol.1975.sp011074
Johnson KG.1. A technique for perfusion of skin has been used to investigate a possible neurochemical basis for the different patterns of sweating in domestic animals. Evaporative water loss was measured from excised trunk skin, ears or tails perfused with a nutrient Krebs solution, to which drugs were added as required. Perfused skin was observed to sweat in response to administration of sudorific drugs, and some features of the patterns of sweating were similar to those which could be induced by heating or by drugs in conscious animals. 2. In sheep and goat skin, injections of adrenaline, and to a less...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/0005-7967(77)90095-x
Schmoldt A, Benthe HF, Haberland G, Sinelnikova EM, Dvoretskova TV, Kagan ZS, Marshall WL, Stoian M, Andrews WR.It has been shown that for the reaction catalyzed by "biodegradative" L-threonine dehydratase from E. coli strains K-12 and 980 in 0.5 M phosphate-carbonate buffer, pH 8.4 and pH 9.5, the plots of initial reaction rate (v) versus the initial substrate concentration ([S]0 are characterized by several inflection points, i. e. an intermediate plateau. The plot of v versus the allosteric activator (AMP) concentration have very complicated shapes: there are several inflection points, and also the maximum at L-threonine concentration equal to 3-10(2) and 5-10(-2) M. High AMP concentrations inhibit t...
Digitoxin metabolism by rat liver microsomes.
Biochemical pharmacology    September 1, 1975   Volume 24, Issue 17 1639-1641 doi: 10.1016/0006-291x(75)90200-4
Schmoldt A, Benthe HF, Haberland G, Jallon JM, Risler Y, Iwatsubo M, Karuzina II, Bachmanova GI, Kuznetsova GP, Izotov MV, Archakov AI, Kröger H....It has been found that NADPH-dependent hydroxylation of dimethylaniline, aniline, p- and o-nitroanisol and lipid peroxidation is inhibited by the tyrosine-copper (II) complex (low molecular weight analog of superoxide dismutase), which is indicative of a possibility of superoxide radicals formation in these reactions. The inhibition of the above-mentioned reactions with Tyr2-Cu2+ is less pronounced or absent, if cumole hydroperoxide is used as cosubstrate instead of NADPH. Differences in the Tyr2-Cu2+ complex effects on the cumule hydroperoxide-dependent xenobiotics hydroxylation and lipid per...
Immunological and chemical correlation between alpha-fetoproteins from human and several mammalian species.
Annals of the New York Academy of Sciences    August 22, 1975   Volume 259 109-118 doi: 10.1111/j.1749-6632.1975.tb25407.x
Nishi S, Watabe H, Hirai H.Alpha-Fetoproteins of several animals were purified and their molecular weights, amino acid compositions and peptide maps were compared, demonstrating the close similarities. These data indicated that the alpha-fetoproteins of mammalian species have closely related antigenical and chemical structures. Rabbits and horses were immunized with human alpha-fetoprotein, and it was observed that the animals produced antibodies reaction not only with human alpha-fetoprotein but with their homologous alpha-fetoproteins. The results were interpreted as the breakdown of the tolerance to their own alpha-f...
Leucocyte myosin and its location in the cell.
Biochimica et biophysica acta    August 19, 1975   Volume 400, Issue 2 222-243 doi: 10.1016/0005-2795(75)90177-4
Shibata N, Tatsumi N, Tanaka K, Okamura Y, Senda N.The intracellular location of the binding site of antibody against purified myosin prepared from equine leucocytes was investigated in neutrophils and lymphocytes by electron microscopy using peroxidase-labelled antibody method. The myosin extracted from equine leucocytes could bind skeletal muscle F-actin and the formed complex showed the biophysical and biochemical properties and electron microscopic appearance of actomyosin. On immunodiffusion, the leucocyte myosin formed a single precipitin line with its antibody prepared in rabbits. The antibody also formed single precipitin lines with my...
Binding of hexachlorobenzene to erythrocytes: species variation.
Life sciences    August 15, 1975   Volume 17, Issue 4 545-549 doi: 10.1016/0024-3205(75)90088-0
Yang RS, Coulston F, Golberg L.No abstract available
Conformational energy refinement of horse-heart ferricytochrome c.
Biochemistry    August 12, 1975   Volume 14, Issue 16 3509-3517 doi: 10.1021/bi00687a001
Warme PK, Scheraga HA.The reported X-ray structure of horse-heart ferricytochrome c has been refined by conformational energy calculations, using a three-stage computational procedure. In stage I, the atomic positions are adjusted to conform to idealized bond lengths and bond angles characteristic of small amino acid derivatives, while yet remaining as close as possible to the X-ray coordinates. In stage II, atomic overlaps are eliminated by adjusting the backbone and side-chain dihedral angles to minimize the nonbonded energy, hydrogen-bonded energy, and rotational energy contributions. In the final stage of refin...
The influence of amino acid substitutions on the conformational energy of cytochrome c.
Biochemistry    August 12, 1975   Volume 14, Issue 16 3518-3526 doi: 10.1021/bi00687a002
Warme PK.Conformational energies have been evaluated for each of the staggered side-chain conformations associated with the 261 amino acid substitutions known to occur among 60 eucaryotic species. At least 86% of these substitutions can be sterically accommodated (one at a time) within the structure of horse-heart cytochrome c resulting from conformational energy refinement. Simultaneous incorporation of all pertinent amino acid substitutions found in eight representative species into the refined horse-heart structure is also shown to be sterically possible, with few exceptions. In two cases (Pekin duc...
[Ultrastructural and enzyme studies on trained and untrained horse muscles].
Schweizer Archiv fur Tierheilkunde    August 1, 1975   Volume 117, Issue 8 453-457 
Straub R, Howald H, Gerber H, Diehl M, Pauli B.No abstract available
Glucose utilization and contribution to milk components in lactating ponies.
Journal of animal science    August 1, 1975   Volume 41, Issue 2 568-571 doi: 10.2527/jas1975.412568x
Anwer MS, Gronwall R, Chapman TE, Klentz RD.No abstract available
Influence of mare uterine tubal fluids on the metabolism of stallion sperm.
American journal of veterinary research    August 1, 1975   Volume 36, Issue 08 1149-1152 
Engle CE, Foley CW, Witherspoon DM, Scarth RD, Goetsch DD.Three experiments were conducted on the metabolism of stallion sperm. In experiment 1, whole and washed sperm were incubated under aerobic and anaerobic enviroments and analyzed before and after controlled incubation for motility, pH, lactic acid, glucose, fructose, and O2 comsumption. In experiment 2, whole and washed sperm were incubated aerobically and anaerobically with and without uterine tubal fluids. Experiment 3 was the same as experiment 2, except added substrates of glucose and lactic acid were studied. The same examinations were made in experiments 2 and 3 as for experiment 1. Motil...
Differences in subunit composition and iron content of isoferritins.
The Journal of biological chemistry    July 25, 1975   Volume 250, Issue 14 5446-5449 
Ishitani K, Listowsky I.Horse spleen ferritin was fractionated into its constituent isoferritins by isoelectric focusing. Separated isoferritins were stable and showed no tendency to redistribute when re-examined by analytical gel focusing. All of the isoferritins were immunologically indistinguishable when tested with antibodies raised against unfractionated horse spleen ferritin. The separated isoferritins also had similar conformations as determined by circular dichroism. Iron distribution studies, however, revealed a wide disparity among the isoferritins. The most acidic components had the lowest iron content but...
Effect of oral or caecal administration of protein supplements on equine plasma amino acids.
The British veterinary journal    July 1, 1975   Volume 131, Issue 4 466-473 
Reitnour CM, Salsbury RL.No abstract available
ATPase activity and filament formation of partially purified myosin from leucocytes.
Journal of biochemistry    July 1, 1975   Volume 78, Issue 1 93-103 
Takeuchi K, Shibata N, Senda N.Myosin was isolated from leucocytes in horse arterial blood by the same procedures used for the isolation of myosin from skeletal muscle. The Ca2+-, EDTA-, and Mg2+-ATPase [EC 3.6.1.3] activities of the protein was 0.148, 0.147, and 0.001 mumoles/min/mg, respectively, in 0.5 M KCl at pH 7.0 and 25 degrees. The Ca2+-ATPase activity decreased with decrease in the ionic strength. No difference was found between leucocyte myosin and skeletal myosin in the pH profiles of Ca2+- and EDTA-ATPases. The rate and amount of the initial burst of Pi liberation of leucocyte myosin were 0.002 mumoles/min/mg a...
Pregnant mare serum gonadotrophin: rate of clearance from the circulation of sheep.
Journal of reproduction and fertility    July 1, 1975   Volume 44, Issue 1 95-100 doi: 10.1530/jrf.0.0440095
McIntosh JE, Moor RM, Allen WR.The process involved in the disappearance of PMSG from the blood of sheep, following a single intravenous injection, has been separated into two exponential components. Values (mean plus or minus S.E.) calculated from experiments on five animals were: metabolic clearance rate (37.8 plus or minus 1.6 ml hr-minus 1); rate constant of disposal (0.0315 plus or minus 0.0016 hr-minus 1); half-time of disposal (21.2 plus or minus 1.1 hr). The stage of the oestrous cycle, ovariectomy and the dose of PMSG used had no apparent effect on these values.
Effects of histamine and acetylcholine on equine digital lymph flow and composition. Robinson NE, Jones GA, Scott JB, Dabney JM.We measured the flow rate and protein concentration of lymph collected from a digital lymphatic in eight anesthetized ponies. Additionally, we recorded systemic arterial pressure (Part), and small vein pressure (Psv). Control lymph flow averaged 0.068 ml/min, and contained 3.11 g/100 ml of protein with albumin/globulin ratio of 0.75. Twenty-minute local intra-arterial infusion of acetylcholine (10 mug/min.) elevated Psv but did not increase lymph flow rate or protein concentration. A 60-min local intra-arterial infusion of histamine (10 mug/min) produced a marked sustained increase in Psv and ...
The influence of exercise on serum enzyme levels in the horse.
Equine veterinary journal    July 1, 1975   Volume 7, Issue 3 160-165 doi: 10.1111/j.2042-3306.1975.tb03258.x
Anderson MG.A group of clinically normal horses was subjected to controlled strenuous exercise. Elevated serum concentrations of lactic dehydrogenase, aldolase and creatine kinase were observed after exercise but no significant change in serum glutamic-oxalacetic transaminase was noted. These changes were reduced by repeated exposure to exercise suggesting that measurement of serum enzyme elevations, particularly creatine kinase, might be a useful index of fitness in the horse. Administration of prednisolone prior to exercise also reduced these changes. Since the serum enzyme concentrations had returned t...
Nitrite and nitrate pharmacokinetics in the dog, sheep, and pony.
American journal of veterinary research    July 1, 1975   Volume 36, Issue 7 941-947 
Schneider NR, Yeary RA.Elimination kinetics of nitrite and nitrate in the dog, sheep, and pony were determined. The elimination half-lives of nitrite were 0.499, 0.475, and 0.566 hours in the dog, sheep, and pony, respectively; those of nitrate were 44.681, 4.233, and 4.821 hours. Apparent specific volumes of distribution (V'd) of nitrite were variable among the 3 species--1,623.7 ml/kg in the dog, 278.0 ml/kg in the sheep, and 191.6 ml/kg in the pony. The V'd of nitrate were less varied--dog, 238.5 ml/kg; sheep, 291.1 ml/kg; and pony, 209.3 ml/kg. In the in vitro studies on protein binding in canine plasma, the ext...
Inhibition of horse muscle acylphosphatase by pyridoxal 5′-phosphate.
Biochimica et biophysica acta    June 24, 1975   Volume 391, Issue 2 486-493 doi: 10.1016/0005-2744(75)90272-7
Ramponi G, Manao G, Camici G, White GF.It has been shown that horse muscle acylphosphatase is inhibited by pyridoxal 5'-phosphate and that the inhibition is pH dependent, reversible and competitive with respect to substrate binding. Spectral analysis on the EI complex demonstrates the presence of a Schiff base. Reduction of the pyridoxal 5'-phosphate-inhibited enzyme with sodium borohydride, followed by amino acid analysis, produces a diminution of the free lysine peak and the appearance of a new peak corresponding to epsilon-pyridoxyllysine. The results suggest that there is at least one NH2-lysyl residue of horse muscle acylphosp...
Structure of horse-spleen apoferritin at 6 angstom resolution.
Nature    June 19, 1975   Volume 255, Issue 5510 653-654 doi: 10.1038/255653a0
Hoare RJ, Harrison PM, Hoy TG.No abstract available
Heat stability and reactivation of mare milk lysozyme.
Journal of dairy science    June 1, 1975   Volume 58, Issue 6 835-838 doi: 10.3168/jds.S0022-0302(75)84646-7
Jauregui-Adell J.Mare milk and aqueous solution of mare milk lysozyme were incubated for variable times between 30 C and 100 C at pH 3, 6, or 9. Lysozyme activity was stable at acid and neutral pH and labile at alkaline pH. Some of the results show the existence of a reactivation process in mare's milk and in aqueous solution. reaching 30 to 40% after incubation of the aqueous solution at 4 C for 20 days at pH 3 or 6.
Proceedings: The oxygen affinity of horse and human myoglobins.
The Journal of physiology    June 1, 1975   Volume 248, Issue 1 32P-33P 
Boulton FE, Holly JM.No abstract available
Constituents of ceramide monohexoside isolated from equine kidney.
The Japanese journal of experimental medicine    June 1, 1975   Volume 45, Issue 3 231-234 
Kojima H, Tamai Y.No abstract available
Biochemistry, cytology, and microbiology of equine peritoneal fluid after experimental strangulation obstruction of the distal ileum.
The American journal of digestive diseases    June 1, 1975   Volume 20, Issue 6 595 
Hamiliton DP, Hardenbrook HJ.No abstract available
Recovery of procaine from biological fluids.
Research communications in chemical pathology and pharmacology    June 1, 1975   Volume 11, Issue 2 187-194 
Tobin T, Tai CY, Arnett S.A published method for the recovery of procaine from human plasma using 5M NaOH gave very poor recoveries. Investigation showed that under the recommended extraction conditions procaine was rapidly hydrolysed. Extraction into benzene of samples buffered to pH 9.0 with borate buffer allowed essentially 100% recovery of procaine from equine plasma and urine.
Comparison of the myoglobin of the zebra (Equus burchelli) with that of the horse (Equus caballus).
Biochimica et biophysica acta    May 30, 1975   Volume 393, Issue 1 201-204 doi: 10.1016/0005-2795(75)90232-9
Darbre PD, Romero-Herrera AE, Lehmann H.The tryptic and peptic peptides from the myoglobin of the zebra (Equus burchelli) have been compared with those obtained from the myoglobin of the horse (Equus caballus). No differences in the myoglobin were found between these two species.
Bile secretion in ponies with biliary fistuals.
American journal of veterinary research    May 1, 1975   Volume 36, Issue 5 653-654 
Gronwall R, Engelking LR, Anwer MS, Erichsen DF, Klentz RD.Surgically placed bile duct cannulas allowed collection of secreted bile from nonanesthetized ponies. UNINTERRUPTED ENTEROPHEPATIC CIRCULATION WAS PERMITTED BETWEEN COLLECTIONS. Deleterious effects of cannulation were not observed. Average bile flow was 18.6 plus or minus 1.72 (standard error) mul/minute/kg, bile acid excretion was 0.179 plus or minus 0.0212 mumole/minute/kg, and bilirubin excretion averaged 1.22 plus or minus 0.136 mug/minute/kg.
Carboxymethyl horse-liver alcohol dehydrogenase. Ligand-binding and kinetic properties of the cysteine-46-modified enzyme.
Archives of biochemistry and biophysics    May 1, 1975   Volume 168, Issue 1 145-162 doi: 10.1016/0003-9861(75)90237-4
Reynolds CH, McKinley-McKee JS.No abstract available
Separation of progonadotropic and antigonadotropic activities in ovine and equine HCG antisera.
Biology of reproduction    May 1, 1975   Volume 12, Issue 4 516-521 doi: 10.1095/biolreprod12.4.516
Cole HH, Dewey R, Geschwind II, Chapman M.No abstract available
Identification of O-cetylated N-acylneuraminic acids by mass spectrometry.
Carbohydrate research    May 1, 1975   Volume 41 7-17 doi: 10.1016/s0008-6215(00)87002-0
Kamerling JP, Vliegenthart JF.A number of O-acetylated N-acylneuraminic acids, isolated from submandibular glands of cow and horse and from horse erythrocytes, have been characterized by mass spectrometry. On the basis of the typical fragmentation patterns of the pertrimethylsilyl derivatives of the methyl esters of the compounds, they were identified as 4-O-acetyl-, 9-O-acetyl-, 4,9-di-O-acetyl-, and 7,9-di-O-acetyl N-acetylneuraminic acid, and 4-O-acetyl-and 9-O-acetyl-N-glycolylneuraminic acid.