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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.
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...
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...
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
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
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.
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
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.
Manganese-substituted hemoglobin and myoglobin.
Annals of the New York Academy of Sciences    April 15, 1975   Volume 244 174-186 doi: 10.1111/j.1749-6632.1975.tb41530.x
Hoffman BM, Gibson QH, Bull C, Crepeau RH, Edelstein SJ, Fisher RG, McDonald MJ.No abstract available
The use of prostaglandins in reproduction.
The Canadian veterinary journal = La revue veterinaire canadienne    April 1, 1975   Volume 16, Issue 4 97-101 
Wenkoff MS.No abstract available
Species variability in the modification of erythrocyte surface proteins by enzymatic probes.
Biochimica et biophysica acta    March 13, 1975   Volume 382, Issue 2 181-192 doi: 10.1016/0005-2736(75)90176-5
Carraway KL, Colton DG, Shin BC, Triplett RB.Bovine and equine erythrocytes have been studied by three different surface modification techniques to investigate the accessibility of the surface components to the external medium. Lactoperoxidase labeling of equine erythrocytes results in a significant labeling of only one membrane component, a 100 000-mol.wt polypeptide corresponding to the membrane-spanning Component III of human erythrocytes. The major sialoglycoprotein of the equine erythrocyte is not labeled. This is in contradistinction to the situation for human and bovine cells, where both components are labeled. The equine membrane...
Hemoglobin genetics in bovines and equines.
Indian journal of biochemistry & biophysics    March 1, 1975   Volume 12, Issue 1 51-57 
Lalthantluanga R, Gulati JM, Barnabas J.No abstract available
Mercuri-nitrophenol as a reporter group for the conformational change of hemoglobin.
Journal of biochemistry    March 1, 1975   Volume 77, Issue 3 595-604 doi: 10.1093/oxfordjournals.jbchem.a130761
Yagisawa S.One mole of horse hemoglobin tetramer reacts with 2 moles of 2-chloromercuri-4-nitrophenol (MNP) at beta 93 cysteine. The difference spectra between NMP-bound hemoglobin and hemoglobin, measured with the aid of ascorbic acid and ascorate oxidase [EC 1.10.3.3] as deoxygenation reagents, indicate that the pK of the phenolic hydroxyl group of MNP increases by 0.6 to 0.8 pH unit on deoxygenation of the hemoglobin. The Hill constant of the modified hemoglobin changes with pH. It decreases from about 2.4 at pH 6.8 to about 1.0 at pH 9.0 This effect of the reagent is interpreted as inherent to the re...
Comparative analyses of members of the Venezuelan equine encephalomyelitis virus complex.
American journal of epidemiology    March 1, 1975   Volume 101, Issue 3 245-252 doi: 10.1093/oxfordjournals.aje.a112092
Pedersen CE, Eddy GA.Polyacrylamide gel electrophoretic examination of viruses selected from the Venezuelan equine encephalomyelitis (VEE) complex revealed distinct strain to strain differences in profiles of the two virion envelope proteins. The core protein was identical in all viruses tested. We detected five electrophoretic patterns into which the virus strains could be classified and these were designated alpha (alpha), beta (beta), gamma (gamma), delta (delta), and episolon (episolon). Isolates representing variant E of subtype I exhibited a profile characterized by only one apparent envelope band. The epizo...
Identification of the lysine residue modified during the activation of acetimidylation of horse liver alcohol dehydrogenase.
Biochemistry    January 28, 1975   Volume 14, Issue 2 200-203 doi: 10.1021/bi00673a002
Dworschack R, Tarr G, Plapp BV.A single amino group in horse liver alcohol dehydrogenase was modified with methyl(14C)acetimidate by a differential labeling procedure. Lysine residues outside the active site were modified with ethyl acetimidate while a lysine residue in the active site was protected by the formation of an enzyme-NAD+-pyrazole complex. After the protecting reagents were removed, the enzyme was treated with methyl(14C)acetimidate. Enzyme activity was enhanced 13-fold as 1.1 (14C)acetimidyl group was incorporated per active site. A labeled peptide was isolated from a tryptic-chymotryptic digest of the modified...
Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study.
Biochimica et biophysica acta    January 23, 1975   Volume 377, Issue 1 1-8 doi: 10.1016/0005-2744(75)90279-x
Bull TE, Lindman B, Einarsson R, Zeppezauer M.The binding of Au(CN)2- and Pt(CN)4-2- ions to the coenzyme binding site of horse liver alcohol dehydrogenase (alcohol : NAD+ oxidoreductase EC 1.1.1.1) has been studied by 35C1 nuclear magnetic relaxation. Longitudinal relaxation rates were analyzed in terms of a simple model and binding constants for Au(CN)2-, Pt(CN)4-2- and C1- were estimated. From a comparison between transverse and longitudinal relaxation rates the correlation time and the quadrupole coupling constant of bound chloride ion were obtained. The quadrupole coupling constant estimated from a simple electrostatic model for chlo...
Conformational studies of equilibrium structures in fragments of horse heart cytochrome c.
European journal of biochemistry    January 2, 1975   Volume 50, Issue 2 367-374 doi: 10.1111/j.1432-1033.1975.tb09812.x
Toniolo C, Fontana A, Scoffone E.Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
Molecular properties of multiple forms of acid phosphatase from horse liver.
Acta biochimica Polonica    January 1, 1975   Volume 22, Issue 3 201-209 
Wasyl Z.1. Horse liver acid phosphatase was separated into two partially purified fractions differing in molecular weight (enzyme I about 100 00, enzyme II about 25 000). 2. Enzyme I was separated into several subfractions by DEAE-cellulose chromatography and isoelectric focusing. 3. Molecular weight, sedimentation coefficient and effective molecular radii were determined for acid phosphatases I and II by gel filtration and density-gradient centrifugation.
Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 66.
Biochemical and biophysical research communications    December 23, 1974   Volume 61, Issue 4 1400-1406 doi: 10.1016/s0006-291x(74)80439-0
Corradin G, Harbury HA.No abstract available
Horse hemoglobin polymorphism.
Annals of the New York Academy of Sciences    November 29, 1974   Volume 241 61-69 doi: 10.1111/j.1749-6632.1974.tb21866.x
Clegg JB.No abstract available
Photooxidation of horse and sperm-whale myoglobin sensitized by the heme group.
Photochemistry and photobiology    October 1, 1974   Volume 20, Issue 4 357-369 doi: 10.1111/j.1751-1097.1974.tb06588.x
Folin M, Gennari G, Jori G.The irradiation of horse and sperm-whale Fe” or Fez’ myoglobins with visible light showed that axial ligands that render the heme diamagnetic (e.g. 02, CO or CN-) endow the hemoproteins with a marked photosensitivity. In contrast, high-spin myoglobins are unaffected by visible light. These findings appear to be of general validity for all hemo-proteins and are in agreement with the involvment of the triplet state of the heme as the reactive intermediate. In all cases, the overall photoprocess occurs within a very narrow spatial range, leading to specific modification of these photoox...
The role of disulfide reduction in chromatin release from equine sperm.
The Journal of experimental zoology    September 1, 1974   Volume 189, Issue 3 387-393 doi: 10.1002/jez.1401890311
Wagner TE, Mann DR, Vincent RC.No abstract available
A steady-state kinetic model of butyrylcholinesterase from horse plasma.
The Biochemical journal    September 1, 1974   Volume 141, Issue 3 825-834 doi: 10.1042/bj1410825
Augustinsson KB, Bartfai T, Mannervik B.The steady-state kinetics of the butyrylcholinesterase-catalysed hydrolysis of butyrylthiocholine and thiophenyl acetate were shown to deviate from Michaelis-Menten kinetics. The ;best' empirical rate law was selected by fitting different rate equations to the experimental data by non-linear regression methods. The results were analysed in view of two alternative interpretations: (1) the reaction is catalysed by a mixture of enzymes, or (2) the activity is due to a single enzyme displaying deviations from Michaelis-Menten kinetics. It was concluded that the second alternative applies, and this...
Characterization of the forssman glycolipid hapten of horse kidney by mass spectrometry.
The Journal of biological chemistry    August 10, 1974   Volume 249, Issue 15 4819-4823 
Karlsson KA, Leffler H, Samuelsson BE.No abstract available
Molecular weight of the major acidic glycoprotein of horse erythrocyte membrane.
Archives of biochemistry and biophysics    August 1, 1974   Volume 163, Issue 2 581-588 doi: 10.1016/0003-9861(74)90517-7
Hunter SJ, Fletcher MA, Bush CA.No abstract available
Horse pancreatic ribonuclease.
European journal of biochemistry    July 15, 1974   Volume 46, Issue 2 221-233 doi: 10.1111/j.1432-1033.1974.tb03615.x
Scheffer AJ, Beintema JJ.No abstract available
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.
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Proceedings of the National Academy of Sciences of the United States of America    July 1, 1974   Volume 71, Issue 7 2892-2894 doi: 10.1073/pnas.71.7.2892
Wilgus H, Stellwagen E.Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the ...
Purification and antigenicity of an M-like protein of Streptococcus equi.
Infection and immunity    July 1, 1974   Volume 10, Issue 1 116-122 doi: 10.1128/iai.10.1.116-122.1974
Woolcock JB.A cell wall component of Streptococcus equi analogous to the M protein of group A streptococci has been identified and purified. A highly purified product has been obtained from cells by hot acid extraction, followed by acid precipitation, ammonium sulfate fractionation, and column chromatography. This product reacts with S. equi antiserum. The existence of this fraction in S. equi has been confirmed by the failure of trypsin-treated cells and their extracts to remove the long-chaining capacity of S. equi antiserum. The antigenicity of this M-like protein when incorporated in adjuvant has been...
Equine hepatic and renal metallothioneins. Purification, molecular weight, amino acid composition, and metal content.
The Journal of biological chemistry    June 10, 1974   Volume 249, Issue 11 3537-3542 
Kägi JH, Himmelhoch SR, Whanger PD, Bethune JL, Vallee BL.No abstract available