Analyze Diet

Topic:Bioinformatics

Bioinformatics in horses involves the application of computational tools and techniques to analyze and interpret biological data related to equine species. This interdisciplinary field integrates biology, computer science, and information technology to study genetic, genomic, and proteomic information in horses. Bioinformatics can be used to investigate genetic variations, understand disease mechanisms, and assist in the development of targeted therapies and breeding programs. Key areas of focus include genome sequencing, gene expression analysis, and the identification of genetic markers associated with specific traits or conditions. This page compiles peer-reviewed research studies and scholarly articles that explore the application and impact of bioinformatics on equine genetics, health, and breeding.
Horse erythrocyte gangliosides: preparation of the major hematoside NeuNG1-Lac-Cer.
Lipids    September 1, 1980   Volume 15, Issue 9 682-685 doi: 10.1007/BF02534019
Maget-Dana R, Michalski JC.A simple method for the isolation of hematoside NeuNG1-Lac-Cer from horse erythrocytes is described. An aliquot of the crude ganglioside fraction was labeled by tritiated sodium borohydride after mild periodate oxidation. The compounds obtained were used as radioactive tracers in column chromatography. Gangliosides were applied onto a silicic acid column and eluted stepwise by solvents of steadily increasing polarity. The major ganglioside, NeuNG1-Lac-Cer, was eluted in a high yield by the solvent mixture chloroform/methanol/water (60:35:8, v/v/v).
Assembly of intra- and interspecies hybrid apoferritins.
The Journal of biological chemistry    July 10, 1980   Volume 255, Issue 13 6234-6237 
Otsuka S, Listowsky I, Niitsu Y, Urushizaki I.An intraspecies hybrid apoferritin was assembled by mixing subunits of horse heart ferritin, which consists mainly of H-type subunits, and horse spleen ferritin, in which L-type subunits predominate. Interspecies hybrid apoferritins were reconstituted from subunits of human liver-horse spleen ferritins and from rat liver-horse spleen ferritins. All the hybrid ferritins migrated as single zones with electrophoretic mobilities intermediate between those of the parent ferritins. Isoelectric focusing data and immunological patterns were consistent with the view that the reassembled apoferritins we...
A biologically active, three-fragment complex of horse heart cytochrome c.
The Journal of biological chemistry    February 10, 1980   Volume 255, Issue 3 845-853 
Juillerat M, Parr GR, Taniuchi H.No abstract available
Identification and genetics of horse lymphocyte alloantigens.
Immunogenetics    January 1, 1980   Volume 11, Issue 5 499-506 doi: 10.1007/BF01567818
Bailey E.Six hundred horses were tested with lymphocytotoxic antisera derived from 550 parous mares and 58 antisera produced by alloimmunization with horse blood cells. Seven equine lymphocyte specificities were identified using correlation analysis of the test data, absorption analysis and lysostripping. These specificities are expressed on lymphocytes and platelets, but not on red blood cells (RBC). Therefore, these specificities do not appear to be products of any of the eight known blood group systems of the horse. The distribution of these specificities in 113 Thoroughbred horses and 57 Arabian ho...
Insensitivity of the ferritin iron core to heat treatment.
Experientia    March 15, 1979   Volume 35, Issue 3 300-301 doi: 10.1007/BF01964311
Bertrand ML, Harris DC.To test whether the reactivity of ferritin iron is affected by the heat treatment used in ferritin isolation, we prepared ferritin from the same horse spleen with or without heating. Both samples exhibited similar reactivity upon reduction or chelation of iron.
The amino acid sequence of equine metallothioneins.
Experientia. Supplementum    January 1, 1979   Volume 34 153-161 doi: 10.1007/978-3-0348-6493-0_6
Kojima Y, Berger C, Kägi JH.No abstract available
A detection tube for cholinesterase inhibiting compounds.
International journal of environmental analytical chemistry    January 1, 1979   Volume 6, Issue 2 89-94 doi: 10.1080/03067317908071163
Barendsz AW.The enzyme butyrylcholinesterase from horse serum catalyses the hydrolysis of certain esters. The orange-red 2,6-dichloroindophenyl acetate will be converted by the enzyme into a deep blue alcohol. The colour transformation does not occur when the enzyme is inactivated. By making use of this biochemical reaction a cheap and simple, but very sensitive and specific detection tube could bedeveloped. The tube comprises a breakable ampoule with an aqueous buffer solution, a freeze-dried preparation of the chromogenic ester with a filler promoting its dissolution, a freeze-dried preparation of butyr...
Biochemical changes in horses during endurance rides.
The Veterinary record    May 27, 1978   Volume 102, Issue 21 469 doi: 10.1136/vr.102.21.469
Orton RG.No abstract available
Ferritin: structure, biosynthesis, and role in iron metabolism.
Physiological reviews    April 1, 1978   Volume 58, Issue 2 317-396 doi: 10.1152/physrev.1978.58.2.317
Munro HN, Linder MC.No abstract available
Enzymes in organic synthesis. Influence of substrate structure on rates of horse liver alcohol dehydrogenase-catalysed oxidoreductions.
Journal of the Chemical Society. Perkin transactions 1    January 1, 1978   Volume 12 1636-1642 doi: 10.1039/p19780001636
Irwin AJ, Lok KP, Huang KW, Jones JB.No abstract available
Methods for quantifying mammalian spermatogenesis: a review.
Journal of animal science    May 1, 1977   Volume 44, Issue 5 818-833 doi: 10.2527/jas1977.445818x
Berndtson WE.No abstract available
Amino acid composition of casein isolated from the milks of different species.
Canadian journal of zoology    January 1, 1977   Volume 55, Issue 1 231-236 doi: 10.1139/z77-026
Lauer BH, Baker BE.Casein was isolated from the milks of the following species: cow, horse, pig, reindeer, caribou, moose, harp seal, musk-ox, polar bear, dall sheep, and fin whale. The caseins were subjected to acid hydrolysis, the resultant amino acids were converted to their n-butyl-N-trifluoroacetyl esters, and the amino acid composition of the caseins was determined by gas chromatographic analysis of these esters. Notable among the results was the close similarity, with respect to amino acid composition, of reindeer and caribou caseins. The results of the amino acid analyses of the other caseins are present...
[Distribution of surface electric potentials in the horse heart].
Veterinarni medicina    October 1, 1976   Volume 21, Issue 10 623-631 
Chvátal O, Hanák J.Surface electric potentials of the heart of four horses were measured by use of unipolar leak with the so called central Wilson's clip; the measurements were performed on 95 precisely fixed places of the equine body. Potentials found out in this way were re-measured with bipolar leaks: the negative electrode was fixed in the place of the highest negative potentials, the positive electrode was gradually attached to places with the highest values of positive potentials. The largest potential differences when the negative electrode was placed in the region of the heart were obtained from the regi...
[Study of hydrolysis of aminoalcohol ethers, phenol and choline under the action of horse blood serum cholinesterase].
Biokhimiia (Moscow, Russia)    October 1, 1976   Volume 41, Issue 10 1773-1777 
Kundriutskova LA, Kruglikova RI.Hydrolysis of ethers of saturated and unsaturated alcohols and ethers, e.g. phenol and choline, under the action of horse blood serum cholinesterase, was studied. The reactivity towards enzymatic hydrolysis is decreased due to a greater length of the chain in the alcohol residue of the benzoic acid aminoethers; at nCH2 = 4 the compound is a poor substrate. An increase in nydrophobicity of the acyl residue of the ether molecule also leads to a decrease in the Vmax and Km values. In case of cholinesterase substrates, an increase in the molecule hydrophobicity results in an increase of its non-pr...
Catalytic iodination of proteins by horse myeloperoxidase in solid state.
Analytical biochemistry    May 7, 1976   Volume 72 372-379 doi: 10.1016/0003-2697(76)90544-3
Dubin A, Silberring J.No abstract available
Chromosome banding: a modified method for consistent G-banding in cattle, horses and buffaloes.
The Veterinary record    May 1, 1976   Volume 98, Issue 18 358 doi: 10.1136/vr.98.18.358-a
Halnan CR.No abstract available
An examination of graft alteration and recipient response to processed mare cortical bone xenografting.
The Japanese journal of veterinary research    May 1, 1976   Volume 24, Issue 1-2 1-12 
Fujinaga T, Koike T.No abstract available
Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution.
Journal of molecular biology    March 25, 1976   Volume 102, Issue 1 27-59 doi: 10.1016/0022-2836(76)90072-3
Eklund H, Nordström B, Zeppezauer E, Söderlund G, Ohlsson I, Boiwe T, Söderberg BO, Tapia O, Brändén CI, Akeson A.No abstract available
A computer analysis of high frequency disturbances in arterial blood flow.
Computers and biomedical research, an international journal    February 1, 1976   Volume 9, Issue 1 75-88 doi: 10.1016/0010-4809(76)90052-5
McEvoy NM, Pimmel RL, Nerem RM.No abstract available
Carbohydrate composition of horse spleen ferritin.
Biochimica et biophysica acta    November 10, 1975   Volume 411, Issue 1 165-167 doi: 10.1016/0304-4165(75)90295-0
Shinjyo S, Abe H, Masuda M.The carbohydrate composition of horse spleen ferritin was studied. 1 mol of the apoferritin, the protein moiety of ferritin, contains 25 mol of hexose, 3 mol of hexosamine and 10 mol of fucose. Same carbohydrate composition was detected in the apoferritin from iron rich ferritins. These results indicate that horse spleen ferritin is composed of non-identical subunits as regards its carbohydrate composition.
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...
Cytochrome c: a thermodynamic study of the relationship among oxidation state, ion-binding and structural parameters. Cation binding to horse-heart ferrocytochrome c.
European journal of biochemistry    July 15, 1974   Volume 46, Issue 2 387-391 doi: 10.1111/j.1432-1033.1974.tb03631.x
Margalit R, Schejter A.The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability constants are in the range of 5-8 mM-1, and the number of binding sites per protein molecule are 1 to 2. The temperature dependence of the stability constant for the Mg2+-ferrocytochrome system was measured. The thermodynamic parameters were found to be: dH&s = 4-12 kcal/mol, dG;,, (25 "C) = -5.6 kcal/mol and AS&, = +57 calxmol-lx K-I.
Electrical dose for ventricular defibrillation of large and small animals using precordial electrodes.
The Journal of clinical investigation    January 1, 1974   Volume 53, Issue 1 310-319 doi: 10.1172/JCI107552
Geddes LA, Tacker WA, Rosborough JP, Moore AG, Cabler PS.Electrical ventricular defibrillation of heavy subjects (over 100 kg body weight) is uncommon for the human or any animal species. This paper reports trans-chest ventricular defibrillation of subjects ranging in weight from 2.3 to 340 kg using conventional defibrillation current (heavily damped sine wave) of 0.3-30 ms duration. It was found that a body weight-to-electrical-shock strength relationship exists and can be expressed in terms of either electrical energy or peak current. For the duration of current pulse used clinically (3-10 ms), the relationship between energy requirement and body ...
Synthesis of liver ferritin on free and membrane-bound polyribosomes of different sizes.
FEBS letters    December 1, 1973   Volume 37, Issue 2 249-252 doi: 10.1016/0014-5793(73)80471-5
Konijn AM, Baliga BS, Munro HN.No abstract available
The equilibrium unfolding parameters of horse and sperm whale myoglobin. Effects of guanidine hydrochloride, urea, and acid.
The Journal of biological chemistry    July 10, 1973   Volume 248, Issue 13 4623-4634 
Puett D.No abstract available
The biochemistry of ferritin.
British journal of haematology    June 1, 1973   Volume 24, Issue 6 677-680 doi: 10.1111/j.1365-2141.1973.tb01695.x
Crichton RR.The researchers investigated the biochemical properties of ferritin, a protein responsible for iron storage in the body. They identified its distribution and structure, noting variations in different species and tissues. […]
Enzyme changes in ageing mammals.
Gerontologia    January 1, 1973   Volume 19, Issue 2 79-125 doi: 10.1159/000211964
Wilson PD.No abstract available
Purification and physicochemical properties of the pregnant mare serum gonadotropin (PMSG).
Endocrinology    July 1, 1972   Volume 91, Issue 1 101-106 doi: 10.1210/endo-91-1-101
Gospodarowicz D.A highly purified preparation of PMSG has been obtained from fresh serum and from a commercial preparation. Carbohydrate and amino acid compositions have been determined. The carbohydrate content of PMSG is 46.7% and the molecule is rich in Sialic Acid (13.5%). The apparent molecular weight of PMSG has been determined by SDS polyacrylamide gel electrophoresis. A molecular weight of 53,000 has been found for the unreduced and unalkylated molecule. After reduction and alkylation, the molecular weight fell to 23,000. From these values it has been concluded that PMSG is an oligomeric molecule comp...
Structure of horse-muscle phosphoglycerate kinase at 6 angstrom resolution.
Nature: New biology    February 16, 1972   Volume 235, Issue 59 195-198 doi: 10.1038/newbio235195a0
Blake CC, Evans PR, Scopes RK.The single peptide chain of 3-phosphoglycerate kinase is folded into two distinct globular units, only one of which seems to be involved in substrate binding.
Purification of horse serum cholinesterase by preparative polyacrylamide gel electrophoresis.
The Journal of biological chemistry    January 25, 1972   Volume 247, Issue 2 566-571 
Main AR, Tarkan E, Aull JL, Soucie WG.No abstract available