Analyze Diet

Topic:Molecular biology

Molecular biology in horses involves the study of molecular processes and genetic mechanisms that underpin equine physiology and health. This field encompasses the analysis of DNA, RNA, proteins, and other biomolecules to understand gene expression, genetic variation, and cellular functions in horses. Techniques such as genomic sequencing, gene expression profiling, and molecular diagnostics are employed to explore topics like hereditary diseases, performance traits, and immune responses in equines. This page assembles peer-reviewed research studies and scholarly articles that investigate the molecular biology of horses, focusing on genetic research, molecular techniques, and their applications in equine science.
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
[Comparative studies on the biochemical nature of myosin–smooth and skele- tal muscle myosin].
Seikagaku. The Journal of Japanese Biochemical Society    April 1, 1971   Volume 43, Issue 4 185-196 
Yamaguchi M.No abstract available
Chemical and immunochemical properties of two classes of globoside from equine organs.
The Japanese journal of experimental medicine    February 1, 1971   Volume 41, Issue 1 67-81 
Naiki M.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
Occurrence of 19-oxoandrost-4-ene-3,17-dione in the course of oestrogen biosynthesis by equine testicular microsomes.
Acta endocrinologica    January 1, 1971   Volume 67, Issue 4 665-676 doi: 10.1530/acta.0.0670665
Oh R, Tamaoki B.No abstract available
Cholinesterase bonded to paper.
Canadian journal of biochemistry    December 1, 1970   Volume 48, Issue 12 1314-1317 doi: 10.1139/o70-204
Stasiw RO, Brown HD, Hasselberger FX.No abstract available
Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution.
Nature    November 7, 1970   Volume 228, Issue 5271 551-552 doi: 10.1038/228551a0
Bolton W, Perutz MF.No abstract available
Horse haemoglobin polymorphism: evidence for two linked non-allelic alpha-chain genes.
Proceedings of the Royal Society of London. Series B, Biological sciences    November 3, 1970   Volume 176, Issue 1043 235-246 doi: 10.1098/rspb.1970.0041
Clegg JB.No abstract available
Equine antihapten antibody. Studies on the primary structure and conformation of equine immunoglobulins.
Biochemistry    October 27, 1970   Volume 9, Issue 22 4310-4321 doi: 10.1021/bi00824a011
Rockey JH, Montgomery PC, Dorrington KJ.No abstract available
Stabilization of horse globin by protoporphyrin IX and hemin.
The Journal of biological chemistry    October 25, 1970   Volume 245, Issue 20 5395-5403 
Sebring ED, Steinhardt J.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...
Ferritin and ferritin iron measurement in tissues by a quantitative immunoprecipitation technique.
Analytical biochemistry    September 1, 1970   Volume 37, Issue 1 64-72 doi: 10.1016/0003-2697(70)90258-7
Leslie AJ, Kaldor I.No abstract available
Preparation and properties of smooth muscle myosin from horse esophagus.
Biochimica et biophysica acta    September 1, 1970   Volume 216, Issue 2 411-421 doi: 10.1016/0005-2728(70)90233-1
Yamaguchi M, Miyazawa Y, Sekine T.Myosin was prepared from smooth muscle of horse esophagus in good yield (about 15 ° mg/Ioo g tissue) and was designated myosin S. Its properties were compared with those of myosin A from skeletal muscle. The ratio of the absorption of myosin S at 280 nm to that at 26o nm was about 1.8, and the amount of contaminating phosphorus was only o.91 g/io 5 g of myosin S, indicating that the latter is free of nucleic acid. The purity of this protein was examined by ultracentrifugation, gel filtration in the presence of 0.5 M KC1 and 6 M urea and chromatography on DEAE-cellulose columns. These e...
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
Comparative action of various kininogenases on crude horse plasma substrates.
Biochemical pharmacology    June 1, 1970   Volume 19, Issue 6 2083-2090 doi: 10.1016/0006-2952(70)90306-0
Budnitskaya P, Gapanhuk E, Henriques OB.The kininogenase activity of trypsin, plasmin, plasma kallikrein and heated Bothrops venom was compared, using fresh, heated and heat-acid-denatured horse plasma as source of kininogen. The venom kininogenase was found to have the highest activity on fresh horse plasma, followed by plasmin and trypsin which were equally active, and plasma kallikrein which was half as active as plasmin on these substrates. Plasmin and trypsin released more kinin from heat-treated than from fresh plasma whereas kallikrein released half as much as it liberates from fresh plasma. On heat-aciddenatured plasma equal...
Studies on equine immunoglobulins. I. The antigenic structure of horse IgG, its fragments and subunits.
Immunochemistry    May 1, 1970   Volume 7, Issue 5 401-412 doi: 10.1016/0019-2791(70)90222-3
Helms CM, Allen PZ.Immunodiffusion analysis of papain digestion products, heavy and light chains of horse IgG-globulins with several rabbit and anti-horse IgG sera, have permitted the demonstration of five antigenic specificities (Fc1, Fc2, L, Lsp and Fabsp) associated with these equine antigens. Reactivity with anti-Fc1 is shown by both F′c and Fc fragments, while anti-Fc2 reactivity is shown only by Fc fragment. Absorption of anti-Fab serum with L chain Fc fragment provides a reagent (anti-Fabsp) which precipitates only with Fab fragment, IgG-globulin or reduced and alkylated IgG. Upon exposure to deterge...
[Biosynthesis of N-acetyl-O-acetylneuraminic acids. I. Incorporation of (14C) acetate into sections of the submaxillary salivary gland of ox and horse].
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    May 1, 1970   Volume 351, Issue 5 595-602 
Schauer R.No abstract available
Microheterogeneity in ferritin molecules.
Biochimica et biophysica acta    April 28, 1970   Volume 207, Issue 1 256-258 doi: 10.1016/0005-2795(70)90158-3
Drysdale JW.No abstract available
N-Terminal sequences of equine and human immunoglobulin heavy chains.
Biochimica et biophysica acta    February 17, 1970   Volume 200, Issue 2 258-266 doi: 10.1016/0005-2795(70)90169-8
Montgomery PC, Bello AC, Rockey JH.N-terminal tetrapeptides from heavy chains of equine γGab- and γT-globulins, and of human γG and γA myeloma proteins and a γM macroglobulin, have been studied. The equine and human heavy chains lacked free α-amino-terminal groups. After mild alkaline hydrolysis, glutamic acid was identified as the terminal amino acid by reaction with dimethylaminonaphthalenesulfonyl chloride, tentatively identifying pyrrolid-2-one-5-carboxylic acid (PCA) as the unreactive terminal residue of each heavy chain. Peptides lacking a free α-amino group were isolated from subtilisin and pronase digests of the ...
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...
Gene expression in an interspecific hybrid: analysis of hemoglobins in donkey, horse, and mule by peptide mapping.
Biochemical genetics    February 1, 1970   Volume 4, Issue 1 73-85 doi: 10.1007/BF00484019
Isaacs WA.No abstract available
Physicochemical studies of equine infectious anemia virus. IV. Determination of the nucleic acid type in the virus.
Archiv fur die gesamte Virusforschung    January 1, 1970   Volume 31, Issue 3 273-280 doi: 10.1007/BF01253762
Nakajima H, Tanaka S, Ushimi C.No abstract available
Structural comparison of the hemoglobins of the genus Equus with those of ruminants.
The Journal of biological chemistry    December 10, 1969   Volume 244, Issue 23 6533-6542 
Kitchen H, Easley CW.No abstract available
[Covalent structure of horse myoglobin].
European journal of biochemistry    December 1, 1969   Volume 11, Issue 2 267-277 doi: 10.1111/j.1432-1033.1969.tb00769.x
Dautrevaux M, Boulanger Y, Han K, Biserte G.No abstract available
Studies on the structure of ferritin and apoferritin from horse spleen. I. Tryptic digestion of ferritin and apoferritin.
Biochimica et biophysica acta    November 11, 1969   Volume 194, Issue 1 34-42 doi: 10.1016/0005-2795(69)90176-7
Crichton RR.No abstract available
Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases.
The Journal of biological chemistry    November 10, 1969   Volume 244, Issue 21 5967-5971 
Hoagstrom CW, Iweibo I, Weiner H.No abstract available
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
Occurrence and nature of equine and bovine myoglobin dimers.
European journal of biochemistry    August 1, 1969   Volume 10, Issue 1 140-145 doi: 10.1111/j.1432-1033.1969.tb00665.x
Van den Oord AH, Wesdorp JJ, Van Dam AF, Verheij JA.In commercial samples of equine myoglobin and samples of equine and bovine myoglobin prepared in the laboratory, a small amount of the protein was present as an aggregate. The presence of the myoglobin aggregate could be demonstrated by gel filtration on Sephadex G-100 Superfine, which also provided a means of isolating it. Gel filtration on Sephadex G-100 showed the molecular weights of the equine and bovine moyglobin aggregates to be about 35000 and 34000 respectively, thus supporting the hypothesis that they are dimers. This was confirmed for the equine myoglobin by ultracentrifugation meas...