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.
H-exchange behaviour and extent of reversible conformation changes in human, bovine, ovine, porcine and equine growth hormones.
Biochimica et biophysica acta    November 17, 1970   Volume 221, Issue 2 290-296 doi: 10.1016/0005-2795(70)90269-2
Cambiaso CL, Retegui LA, Dellacha JM, Santomé JA, Paladini AC.No abstract available
Serum protein electrophoregram in the thoroughbred in Bogota, Colombia.
The British veterinary journal    November 1, 1970   Volume 126, Issue 11 574-578 doi: 10.1016/s0007-1935(17)48071-7
Mussman HC, Rubiano A.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
The recovery of immunoglobulin G from horses by combination of selective plasmapheresis and forced flow electrophoresis.
Research in veterinary science    September 1, 1970   Volume 11, Issue 5 431-437 
Logan EF, Stenhouse A, Watt JG, Clark AE.No abstract available
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
Serum proteins as a screening test for equine infectious anemia.
Zentralblatt fur Veterinarmedizin. Reihe B. Journal of veterinary medicine. Series B    August 1, 1970   Volume 17, Issue 7 739-746 doi: 10.1111/j.1439-0450.1970.tb01572.x
Ribeiro-Netto A, Haetinger H, Pereira-Lima F, Luz IB, Macruz R.No abstract available
[Nutritional physiology of the horse. 3. Protein values in the gastrointestinal tract of slaughtered horses].
Zeitschrift fur Tierphysiologie, Tierernahrung und Futtermittelkunde    August 1, 1970   Volume 26, Issue 5 245-252 
Altmann HJ, Hertel J, Drepper K.No abstract available
Genetics of horse acidic prealbumins.
Genetics    July 1, 1970   Volume 65, Issue 3 495-503 doi: 10.1093/genetics/65.3.495
Braend M.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
Kinins released from horse heat-acid-denaturated plasma by plasmin, plasma kallikrein, trypsin and Bothrops kininogenase.
Biochemical pharmacology    June 1, 1970   Volume 19, Issue 6 2091-2096 doi: 10.1016/0006-2952(70)90307-2
Gapanhuk E, Henriques OB.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...
Nitrogen metabolism in nonruminant herbivores. I. The influence of nonprotein nitrogen and protein quality on the nitrogen retention of adult mares.
Journal of animal science    May 1, 1970   Volume 30, Issue 5 753-760 doi: 10.2527/jas1970.305753x
Slade LM, Robinson DW, Casey KE.No abstract available
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...
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
Differences in E and S chains from isoenzymes of horse liver alcohol dehydrogenase.
Nature    March 21, 1970   Volume 225, Issue 5238 1133-1134 doi: 10.1038/2251133a0
Jörnvall H.No abstract available
[2 physiological functions of humoral immunity and the 2 proteins which assume it in the horse serum]. Sandor G, Audibert F.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 ...
[Electrophoretic studies of the protein fractions of colostrum and milk of Avelignese breed mares in relation to the period of time after delivery].
Acta medica veterinaria    January 1, 1970   Volume 16, Issue 1 73-88 
Minieri L, Intrieri F.No abstract available
Nutrition and the nervous system in farm animals.
World review of nutrition and dietetics    January 1, 1970   Volume 12 377-412 doi: 10.1159/000387592
Howell JM.No abstract available
Studies of electrophoresis on cellulose acetate membrane of serum proteins from normal horses, sheep and pigs.
Acta veterinaria Scandinavica    January 1, 1970   Volume 11, Issue 2 295-304 doi: 10.1186/BF03547989
Ek N.A method for the rapid electrophoresis on a cellulose acetate membrane of serum proteins from horses, sheep and pigs is discussed. The various main globulin fractions in the serum of these animals were experimentally identified. Normal values for the percentage composition of serum from normal horses, sheep and pigs were calculated. In the horse there was great individual variation in the shape of the β-fraction, assumed to be due to different transferrin types. The mean value for β-globulin of 19.5 % in the horse was higher than for the other two species. The albumin percentage was highest ...
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
Electrophoretic analysis of blood serum and plasma proteins of normal horses.
American journal of veterinary research    December 1, 1969   Volume 30, Issue 12 2237-2240 
Bierer BW.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
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
Studies on equine trypsinogen and trypsin.
The Biochemical journal    October 1, 1969   Volume 114, Issue 4 82P doi: 10.1042/bj1140082pa
Harris CI, Hofmann T.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...
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