Analyze Diet

Topic:Protein

Proteins are essential macromolecules that play diverse roles in the physiology and health of horses. They are composed of amino acids and are involved in various biological processes, including tissue growth, repair, and the synthesis of enzymes and hormones. Dietary proteins are a key component of equine nutrition, influencing muscle development, immune function, and overall performance. Horses require a balanced intake of essential amino acids, which must be obtained through their diet, as they cannot be synthesized endogenously. This page compiles peer-reviewed research studies and scholarly articles that explore the types, functions, and dietary requirements of proteins in horses, as well as their impact on equine health and performance.
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
Heat stability and reactivation of mare milk lysozyme.
Journal of dairy science    June 1, 1975   Volume 58, Issue 6 835-838 doi: 10.3168/jds.S0022-0302(75)84646-7
Jauregui-Adell J.Mare milk and aqueous solution of mare milk lysozyme were incubated for variable times between 30 C and 100 C at pH 3, 6, or 9. Lysozyme activity was stable at acid and neutral pH and labile at alkaline pH. Some of the results show the existence of a reactivation process in mare's milk and in aqueous solution. reaching 30 to 40% after incubation of the aqueous solution at 4 C for 20 days at pH 3 or 6.
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
Separation of progonadotropic and antigonadotropic activities in ovine and equine HCG antisera.
Biology of reproduction    May 1, 1975   Volume 12, Issue 4 516-521 doi: 10.1095/biolreprod12.4.516
Cole HH, Dewey R, Geschwind II, Chapman M.No abstract available
Carboxylesterases (EC 3.1.1). Purification and titration of chicken, sheep, and horse liver carboxylesterases.
Canadian journal of biochemistry    May 1, 1975   Volume 53, Issue 5 536-546 doi: 10.1139/o75-074
Inkerman PA, Scott K, Runnegar MT, Hamilton SE, Bennett EA, Zerner B.Chicken, sheep, and horse liver carboxylesterases have been purified by procedures involving ammonium sulfate fractionation, ion-exchange chromatography and gel filtration on Sephadex. The actual yields of the procedures described were as follows: chicken, 1 g from 2 kg of liver powder (chloroform-acetone); sheep, 200 mg from 400 g of powder (chloroform-acetone); horse, 230 mg from 800 g of powder (acetone). The purified enzymes are free of non-carboxyl-esterase protein as shown by gel electrophoresis, although they do contain electrophoretic variants. The equivalent weight of the chicken enzy...
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
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...
Electrophoretic pattern of serum protein in clinically normal horses and ponies with laminitis.
Veterinary medicine, small animal clinician : VM, SAC    March 1, 1975   Volume 70, Issue 3 337-339 
Kirk GR, Hutcheson DP, Neate S.No abstract available
Digestive physiology of the horse.
Journal of the South African Veterinary Association    March 1, 1975   Volume 46, Issue 1 13-17 
Hintz HF.Recent studies on the digestive physiology of the horse are reviewed. It was suggested that the small intestine is the primary site of digestion and absorption of protein, soluble carbohydrates, most minerals, fats, fat soluble and water soluble vitamins. The large intestine is the primary site of fibre digestion and net water absorption. Significant amounts of phosphorus are also absorbed from the large intestine. Many factors such as rate of passage, processing of feeds, level of intake, work and maturity of plant may influence digestive ability.
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.
Immunological characteristics of proteins and enzymes from plasma of full stallion semen.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 11 761-764 
Balbierz H, Bielański W, Kosiniak K, Nikolajczuk M.No abstract available
Immunological characteristics of proteins and enzymes from glandular secretions of particular segments of the reproductive organ in stallions.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 12 833-837 
Balbierz H, Bielański W, Kosiniak A, Nikolajczuk M.No abstract available
Immunological characteristics of proteins and enzymes from semen plasma of stallions collected fractionwise.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1975   Volume 23, Issue 11 765-766 
Balbierz H, Bielański W, Kosiniak K, Nikolajczuk M.No abstract available
Studies on equine immunoglobulins. IV. Immunoglobulins of the donkey.
Immunology    January 1, 1975   Volume 28, Issue 1 187-197 
Allen PZ, Dalton EJ.Donkey IgGa was isolated in purified form from normal and immune donkey sera by column chromatography on DEAE-cellulose. Isolated donkey IgGa and mixtures of (IgGa+IgGb) were used as antigens to prepare rabbit reagents specific for equine IgGa or IgGb. Antibodies present in sera obtained from a single donkey at various times during the course of hyperimmunization with BSA were isolated by immuno-adsorption. The class or subclass of immunoglobulins present among isolated, donkey anti-BSA antibodies was determined by use of specific rabbit anti-equine immunoglobulin reagents. The homologues of h...
The application of polyvalent horse immune sera for electroimmunodiffusion methods.
Annales immunologiae Hungaricae    January 1, 1975   Volume 18 109-113 
Péterfy F, Varró R, Fatrai Z, Barna I, Kiss I.Horse immune sera do not give satisfactory results in immunochemical techniques based on electrophoresis of antigens through antibody-containing agarose gel. As the majority of precipitating horse antibodies belongs to the beta globulins, they migrate in the gel during electrophoresis. After enzymatic treatment the pepsin fragments work well in all electroimmunodiffusion methods.
Cobalt metabolism in horse. Serum level and biosynthesis of vitamin B12.
Acta veterinaria Scandinavica    January 1, 1975   Volume 16, Issue 1 84-94 doi: 10.1186/BF03546698
Salminen K.The levels of serum vitamin B were determined on 16 mature partly warm-blooded, partly Finnish rural-race horses by the radioisotopic competitive inhibition assay method. The mean value from three samplings carried out in dupli- or triplicate was 1.54 ± 0.16 ng/ml. The utilization of serum inorganic cobalt for cyanocobalamin synthesis was studied on two geldings, which received a dose of 200 µCi CoGl i.v. A Sephadex G-100 gel filtration was carried out with the serum proteins from serial blood samplings at different time intervals 15 min. to 48 hrs. after administration. The gel filtration s...
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
The purification of cholinesterase from horse serum.
The Biochemical journal    December 1, 1974   Volume 143, Issue 3 733-744 doi: 10.1042/bj1430733
Main AR, Soucie WG, Buxton IL, Arinc E.A relatively simple method is described by which cholinesterase was purified about 19000-fold starting from horse serum. Typically 20 litres of serum were processed to yield 15-18mg of electrophoretically pure cholinesterase in the form of an active salt-free dry powder. The method included two stages: fractionation with (NH(4))(2)SO(4) and ion-exchange chromatography. The (NH(4))(2)SO(4) stage included, in principle, the acid (pH3) step of the Strelitz (1944) procedure. The step took advantage of the stabilizing effect that 33%-satd. (NH(4))(2)SO(4) has on cholinesterase activity at pH3 and i...
Proceedings: Influence of pressure on the reduction of horse heart ferricytochrome c with potassium ferrocyanide.
Archives internationales de physiologie et de biochimie    October 1, 1974   Volume 82, Issue 4 792 
Vandersypen HA, Heremans KA.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...
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
Serum electrolyte and plasma protein alterations in horses used in endurance rides.
Journal of the American Veterinary Medical Association    August 1, 1974   Volume 165, Issue 3 262-264 
Carlson GP, Mansmann RA.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 ...
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