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.
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
Electronic, hydrophobic, and steric effects of binding of inhibitors to the horse liver alcohol dehydrogenase-reduced pyridine coenzyme binary complex.
Biochemistry    January 18, 1972   Volume 11, Issue 2 170-179 doi: 10.1021/bi00752a006
Sarma RH, Woronick CL.No abstract available
Isolation of -1,4 leads to 1,4-glucosyltransferase from horse muscle.
Archivum immunologiae et therapiae experimentalis    January 1, 1972   Volume 20, Issue 5 755-761 
Hutny J, Dzongowska-Dzongu T.No abstract available
A method of three-dimensional analysis of kinematics and co-ordination of equine extremity joints. A photogrammetric approach applying high-speed cinematography.
Acta veterinaria Scandinavica. Supplementum    January 1, 1972   Volume 37 1-133 
Fredricson I, Drevemo S, Moen K, Dandanell R, Andersson B.No abstract available
Relative dye-binding capacity of albumin from several species with HABA, bromocresol green and Spectru AB-2.
Analytical biochemistry    October 1, 1971   Volume 43, Issue 2 575-581 doi: 10.1016/0003-2697(71)90289-2
Pemberton JR, DeJong J.No abstract available
The subunit structure of horse spleen apoferritin. I. The molecular weight of the subunit.
The Journal of biological chemistry    July 10, 1971   Volume 246, Issue 13 4198-4205 
Bryce CF, Crichton RR.No abstract available
On the electron-transfer-coupled proton release of cytochrome c.
Biochimica et biophysica acta    April 6, 1971   Volume 234, Issue 1 57-61 doi: 10.1016/0005-2728(71)90129-0
Czerlinski GH, Dar K.No abstract available
Equine arteritis virus: ferritin-tagging and determination of ribonucleic acid core.
Archiv fur die gesamte Virusforschung    January 1, 1971   Volume 35, Issue 2 290-295 doi: 10.1007/BF01249721
Breese SS, McCollum WH.No abstract available
Structure of dermatan sulfate. VII. The copolymeric structure of dermatan sulfate from horse aorta.
The Journal of biological chemistry    September 25, 1970   Volume 245, Issue 18 4770-4783 
Fransson LA, Havsmark B.The structure of dermatan sulfate-chondroitin sulfate copolymers, isolated from horse aorta, has been examined. It was found that a large proportion of the galactosaminoglycans of this tissue was obtained as a discrete polysaccharide fraction with an L-iduronic acid to D-glucuronic acid ratio of approximately 1: 2. This finding together with infrared data indicated that the polymer contained approximately equimolar proportions of the three repeating disaccharide units glucuronosyl-N-acetylgalactosamine 4-sulfate (A), iduronosyl-N-acetylgalactosamine 4-sulfate (B), and glucuronosyl-N-acet...
Methanol activity o alcohol dehydrogenases from human liver, horse liver, and yeast.
Archives of biochemistry and biophysics    September 1, 1970   Volume 140, Issue 1 52-59 doi: 10.1016/0003-9861(70)90009-3
Mani JC, Pietruszko R, Theorell H.No abstract available
Molecular weight and amino acid composition of equine thrombin.
Journal of biochemistry    August 1, 1970   Volume 68, Issue 2 193-198 doi: 10.1093/oxfordjournals.jbchem.a129346
Inada Y, Matsushima A, Kotoku I, Hossain SA, Shibata K.No abstract available
Horse liver alcohol dehydrogenase. The primary structure of an N-terminal part of the protein chain of the ethanol-active isoenzyme.
European journal of biochemistry    July 1, 1970   Volume 14, Issue 3 521-534 doi: 10.1111/j.1432-1033.1970.tb00319.x
Jörnvall H.No abstract available
[Evaluation of telemetrically derived stress electrocardiograms of the horse using an electronic computer].
Deutsche tierarztliche Wochenschrift    May 1, 1970   Volume 77, Issue 9 211-217 
Reinhard HJ, Zichner M.No abstract available
A comparison of fingerprints of tryptic digests of human, horse and rat apoferritins.
Comparative biochemistry and physiology    February 1, 1970   Volume 32, Issue 3 451-458 doi: 10.1016/0010-406x(70)90462-7
Richter GW, Moppert GA, Lee JC.1. Fingerprints of tryptic digests of apoferritins from a human liver, horse spleens and ACI rat livers were made by means of electrophoresis and chromatography on microcrystalline cellulose, and were compared. 2. All tryptic peptides also present in apoferritins from the human liver and the horse spleens were also present in apoferritin from the rat livers. 3. In the digests of horse and of rat apoferritin there was a peptide that was not present in the digests of human apoferritin. Another peptide was obtained from human and from rat apoferritin, but not from horse apoferritin. 4. T...
Heterogeneity of erythrocyte catalase. Correlations between sulfhydryl group content, chromatographic and electrophoretic properties.
European journal of biochemistry    November 1, 1969   Volume 11, Issue 1 49-57 doi: 10.1111/j.1432-1033.1969.tb00737.x
Mörikofer-Zwez S, Cantz M, Kaufmann H, von Wartburg JP, Aebi H.No abstract available
Zinc isotope exchange in horse liver alcohol dehydrogenase.
Biochemistry    September 1, 1969   Volume 8, Issue 9 3792-3797 doi: 10.1021/bi00837a045
Drum DE, Li TK, Vallee BL.No abstract available