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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.
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
Isolation and characterization of subunits from equine pituitary follicle-stimulating hormone.
The Journal of biological chemistry    June 10, 1974   Volume 249, Issue 11 3527-3531 
Landefeld TD, McShan WH.No abstract available
The photo-oxidation of horse heart cytochrome c and native cytochrome c2 by reaction centres from Rhodopseudomonas spheroides R26.
Biochimica et biophysica acta    April 23, 1974   Volume 347, Issue 1 1-13 doi: 10.1016/0005-2728(74)90194-7
Prince RC, Cogdell RJ, Crofts AR.No abstract available
A cupro-zinc protein with superoxide dismutase activity from horse liver. Isolation and properties.
Comparative biochemistry and physiology. B, Comparative biochemistry    April 15, 1974   Volume 47, Issue 4 767-777 doi: 10.1016/0305-0491(74)90022-4
Albergoni V, Cassini A.No abstract available
Comparison of the acid denaturation of several hemoglobins which differ in amino acid sequence.
Archives of biochemistry and biophysics    April 2, 1974   Volume 161, Issue 2 472-478 doi: 10.1016/0003-9861(74)90329-4
Jones DD, Steinhardt J.No abstract available
The relation between adenylate cyclase activation and cAMP acculumation in the horse thyroid gland stimulated by thyrotropin.
Molecular and cellular endocrinology    April 1, 1974   Volume 1, Issue 2 139-155 doi: 10.1016/0303-7207(74)90006-9
Boeynaems JM, Van Sande J, Pochet R, Dumont JE.No abstract available
Equine luteinizing hormone and its subunits. Isolation and physicochemical properties.
Biochemistry    March 26, 1974   Volume 13, Issue 7 1389-1393 doi: 10.1021/bi00704a012
Landefeld TD, McShan WH.No abstract available
Multiple components of beta-N-acetylhexosaminidase from equine kidney. Their action on glycolipids and allied oligosaccharides.
Journal of biochemistry    March 1, 1974   Volume 75, Issue 3 495-507 doi: 10.1093/oxfordjournals.jbchem.a130418
Seyama Y, Yamakawa T.No abstract available
Intrinsic fluorescence of a protein devoid of tyrosine and tryptophan: horse hepatocuprein.
FEBS letters    February 15, 1974   Volume 39, Issue 2 164-166 doi: 10.1016/0014-5793(74)80042-6
Agro AF, Albergoni V, Cassini A.No abstract available
A sequence restriction in the variable region of immunoglobulin light chains from sharks, birds, and mammals.
Journal of immunology (Baltimore, Md. : 1950)    February 1, 1974   Volume 112, Issue 2 633-640 
Stanton T, Sledge C, Capra JD, Woods R, Clem W, Hood L.No abstract available
On the limited peptic digestion of horse heart cytochrome C. isolation of C-terminal peptide sequences.
International journal of peptide and protein research    January 1, 1974   Volume 6, Issue 3 145-148 doi: 10.1111/j.1399-3011.1974.tb02371.x
Fontana A, Vita C, Toniolo C.No abstract available
The release of iron from horse spleen ferritin to 1,10-phenanthroline.
The Biochemical journal    January 1, 1974   Volume 137, Issue 1 67-70 doi: 10.1042/bj1370067
Hoy TG, Harrison PM, Shabbir M, Macara IG.The rate of release of iron to 1,10-phenanthroline from ferritin fractions of different iron contents has been studied. The experimental results could be interpreted by a simple hypothetical model of the shape of the hydrous ferric oxide micelle at different iron contents, and reasonable correlation obtained between the rate of release and the calculated micelle surface areas. Initial rates of release did not correlate significantly with protein concentration.
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
Proceedings: Relation of cyclic AMP to sperm motility.
Journal of reproduction and fertility    December 1, 1973   Volume 35, Issue 3 591 doi: 10.1530/jrf.0.0350591
Tash J, Mann T.No abstract available