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.
The complete amino acid sequence of human Cu/Zn superoxide dismutase.
FEBS letters    October 20, 1980   Volume 120, Issue 1 53-56 doi: 10.1016/0014-5793(80)81044-1
Barra D, Martini F, Bannister JV, Schininà ME, Rotilio G, Bannister WH, Bossa F.No abstract available
Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms.
The Journal of biological chemistry    October 10, 1980   Volume 255, Issue 19 9196-9204 
Jabusch JR, Bray RP, Deutsch HF.the sequence of the low activity form of equine erythrocyte carbonic anhydrase has been determined. The most common electrophoretic form, designated D, has been found to have five substitutions. Amino acid exchanges in the electrophoretic variants known as A1, A2, B, and T have been found at six other positions. The data do not permit calculation of the number of polymorphic forms of this enzyme. The equine D isozyme and the analogous human enzyme are quite homologous, 211 of their 260 residues, or 81%, being identical.
The disposition of calcium within parathyroid tissue.
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme    September 1, 1980   Volume 12, Issue 9 475-480 doi: 10.1055/s-2007-999176
Glick DM, Mockel J.The disposition of 45Ca was studied in equine parathyroid gland slices. This preparation was shown to be viable by its ability to carry out protein synthesis, by the responsiveness of its respiration to effectors of oxidative phosphorylation, and by its calcium-inhibitable PTH secretion. 45Ca accumulates in the slices as the extracellular calcium is raised through the range in which physiological serum calcium concentration lies. The tissue slices behave as if they have no calcium pump: (a) depriving the cells of energy by treatment with antimycin A does not admit more calcium to the tissue, (...
The complete amino acid sequence of horse muscle acylphosphatase.
The Journal of biological chemistry    July 25, 1980   Volume 255, Issue 14 6868-6874 
Cappugi G, Manao G, Camici G, Ramponi G.The amino acid sequence of horse muscle acylphosphatase is given in the present paper. The carboxymethylated enzyme consists of a single polypeptide chain of 98 amino acid residues with an acetyl group blocking the NH2 terminus and a tyrosine at the COOH terminus. The calculated molecular weight of the native protein, a mixed disulfide with glutathione, is 11,365. The carboxymethylated protein was cleaved by cyanogen bromide. The three expected fragments were purified; moreover, an additional fragment, derived from a partial failure of cleavage at methionine-24, was purified and characterized....
Assembly of intra- and interspecies hybrid apoferritins.
The Journal of biological chemistry    July 10, 1980   Volume 255, Issue 13 6234-6237 
Otsuka S, Listowsky I, Niitsu Y, Urushizaki I.An intraspecies hybrid apoferritin was assembled by mixing subunits of horse heart ferritin, which consists mainly of H-type subunits, and horse spleen ferritin, in which L-type subunits predominate. Interspecies hybrid apoferritins were reconstituted from subunits of human liver-horse spleen ferritins and from rat liver-horse spleen ferritins. All the hybrid ferritins migrated as single zones with electrophoretic mobilities intermediate between those of the parent ferritins. Isoelectric focusing data and immunological patterns were consistent with the view that the reassembled apoferritins we...
[Hemoglobins, XXXIII. Note on the Sequence of the hemoglobins of the horse (author’s transl)].
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    July 1, 1980   Volume 361, Issue 7 1107-1116 
Matsuda G, Maita T, Braunitzer G, Schrank B.The sequence analysis of the slow migrating component of the hemoglobins of horse was repeated with the automatic methode in the sequenator and the sequence of the beta-chains completed. In the alpha-chains the positions of alpha63 and alpha65 (Gly, Ala) and alpha82 and alpha85 (amides) were changed and the remaining 40 sequences of the beta-chains are reported. According to these data and biological contributions of other authors, the biological aspects of the primary structure and the polymorphism of the hemoglobins of the horse are discussed.
Selectivity of oxidase and reductase activity of horse heart cytochrome c.
Biochemical and biophysical research communications    June 30, 1980   Volume 94, Issue 4 1106-1112 doi: 10.1016/0006-291x(80)90533-1
Myer YP, Thallum KK, Pande J, Verma BC.No abstract available
Enzyme-linked immunosorbent assay, using staphylococcal protein A for detecting virus antibodies.
American journal of veterinary research    June 1, 1980   Volume 41, Issue 6 978-980 
Potgieter LN, Rouse BT, Webb-Martin TA.A modification of the indirect enzyme-linked immunosorbent assay (ELISA) was developed which used staphylococcal protein A linked to horseradish peroxidase. Virus antibodies in equine, bovine, porcine, feline, canine, lagomorphic (rabbit), and human sera were detected, using the indirect ELISA in which the antiglobulin enzyme conjugate was replaced by protein A linked to horseradish peroxidase. Results of the ELISA were compared with the results of the serum-virus neutralization test. The application of the test in laboratories performing serologic assays with sera from diverse animal species ...
The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species.
Biochimica et biophysica acta    April 25, 1980   Volume 622, Issue 2 297-307 doi: 10.1016/0005-2795(80)90040-9
Esparza I, Brock JH.The effect of trypsin digestion on iron-saturated and iron-free (apo) human, rabbit, bovine, pig and horse tranferrins has been studied. Iron-binding fragments were produced only from iron-saturated pig and bovine transferrins although some cleavage of the polypeptide chain occurred in all cases. The apo-transferrins were generally degraded to a greater extent than the corresponding iron-saturated proteins. The ability of the different transferrins to donate iron to rabbit reticulocytes varied in the order rabbit approximately pig greater than human approximately horse greater than bovine. Try...
Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c.
Biochemistry    March 18, 1980   Volume 19, Issue 6 1117-1120 doi: 10.1021/bi00547a012
Smith HT, Millett F.Spectrophotometric titrations of five singly modified horse heart ferricytochromes c, specifically (trifluoromethyl)phenylcarbamylated (CF3PhNHCO-) or trifluoroacetylated (CF3CO-) at lysines-13, -72, and -79, were carried out. The CF3PhNHCO-Lys-13, Lys-79, and CF3CO-Lys-79 derivatives all underwent alkaline isomerization with loss of the 695-nm band to low-spin species with an apparent pK of about 8.9, as did the unmodified cytochrome. However, modification of lysine-72 appeared to alter the reaction pathway since the CF3PhNHCO-Lys-72 derivative isomerized to a high-spin form with an apparent ...
Purification by affinity chromatography and characterization of a neutral alpha-glucosidase from horse kidney.
Biochimica et biophysica acta    March 14, 1980   Volume 612, Issue 1 85-96 doi: 10.1016/0005-2744(80)90281-8
Giudicelli J, Emiliozzi R, Vannier C, de Burlet G, Sudaka P.A horse kidney neutral alpha-D-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) was purified about 580-fold with a yield of 33% by an affinity chromatography technique using the p-aminophenyl-beta-D-maltoside, a substrate derivative, as ligand. The purified enzyme, homogeneous in polyacrylamide gel electrophoresis, was a glycoprotein with a molecular weight of 280 000 as calculated by gel filtration and its isoelectric focusing points was found to be pH 4.1. The purified enzyme was able to hydrolyze various substrates having (alpha-1,2), (alpha-1,3), (alpha-1,4), and (alpha-1,6) glu...
The energy and protein requirements of the light horse.
The British veterinary journal    March 1, 1980   Volume 136, Issue 2 116-121 doi: 10.1016/s0007-1935(17)32333-3
Ellis RN, Lawrence TL.No abstract available
Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism.
Biochemistry    February 19, 1980   Volume 19, Issue 4 743-750 doi: 10.1021/bi00545a021
Verheij HM, Volwerk JJ, Jansen EH, Puyk WC, Dijkstra BW, Drenth J, de Haas GH.It is known that His-48 is part of the active center in pancreatic phospholipase. To further elucidate the role of histidine-48 in the active center of pancreatic phospholipase A2, we have modified the enzyme with a number of bromo ketones and methyl benzenesulfonates. Rapid methylation occurred with methyl p-nitrobenzenesulfonate. Methylated phospholipase shows total loss of enzymatic activity whereas binding of substrate and the cofactor Ca2+ remains intact. Amino acid analysis of methylated equine phospholipase showed the loss of the single molecule of histidine and the formation of one mol...
A biologically active, three-fragment complex of horse heart cytochrome c.
The Journal of biological chemistry    February 10, 1980   Volume 255, Issue 3 845-853 
Juillerat M, Parr GR, Taniuchi H.No abstract available
Comparative studies of alpha-lactalbumin and lysozyme: the proteins of kangaroo (Megaleia rufa and Macropus giganteus) and horse (Equus caballus).
Molecular and cellular biochemistry    January 16, 1980   Volume 29, Issue 1 3-9 doi: 10.1007/BF00230951
Bell K, McKenzie HA, Muller V, Shaw DC.As part of a study of the 'whey' proteins of various mammals, a comparison is made of the alpha-lactalbumins and lysozymes of the kangaroo and horse. In the milk of the red kangaroo (Megaleia rufa) there is only one alpha-lactalbumin and it occurs throughout lactation, but no lysozyme has been detected. There are two alpha-lactalbumins in the milk of the grey kangaroo (Macropus giganteus), one, designated alpha-lactalbumin Zone B, is present throughout lactation; the second, designated alpha-lactalbumin Zone A, is present only in late lactation. One lysozyme is also present. The milk of the ho...
[Effects of giving excess protein to horses].
Zentralblatt fur Veterinarmedizin. Reihe A    January 1, 1980   Volume 27, Issue 9-10 746-757 
Meyer H, Pferdekamp M.No abstract available
Variation of acidic prealbumins in the donkey (Equus asinus).
Animal blood groups and biochemical genetics    January 1, 1980   Volume 11, Issue 2 77-80 doi: 10.1111/j.1365-2052.1980.tb01496.x
Braend M, Romagnoli A.Starch gel electrophoresis of 55 donkey serum samples revealed three prealbumin (Pr) phenotypes temporarily designated Pr M, Pr MT and Pr T. The distribution was in agreement with a genetic theory of two codominant alleles of frequencies, PrM = 0.87 and PrT - 0.13. Variation was also observed for proteins migrating with the same rate as the Xh zones in the horse.
Serum quality: an analysis of its components.
Developments in biological standardization    January 1, 1980   Volume 46 17-20 
Macleod AJ, Drummond O.Foetal and new born bovine sera, horse serum, human serum and human plasma, and protein solutions prepared from the by-products of human plasma fractionation have been analysed. Foetal bovine sera were found to have lower total protein (g/l) and % of gamma-globulin than the other sera studied while the potassium (mmol/1) was higher. Protease inhibitors could be detected in all specimens tested.
A new method for the isolation of aminoacylase from mammalian kidneys.
Acta biochimica et biophysica; Academiae Scientiarum Hungaricae    January 1, 1980   Volume 15, Issue 4 287-293 
Szajáni B.Aminoacylase (E.C. 3.5.1.14) was isolated from the kidneys of different mammalian species (horse, cattle, rabbit and pig) by extracting the organ with water and subjecting the extract to heat treatment at 70 degrees C for 10 min, then, after having removed denatured proteins by fractionating those remaining in the solution by ammonium sulfate. The enzyme obtained in this way can either be used directly for practical purposes (e.g. preparation of immobilized aminoacylase) or further purified by chromatography. For the further purification of porcine kidney aminoacylase we applied a combination ...
Quantitative comparisons of acidic prealbumin (PR) phenotypes in horses.
Acta veterinaria Scandinavica    January 1, 1980   Volume 21, Issue 3 380-388 doi: 10.1186/BF03546870
Ek N, Braend M.Comparisons of Pr protein amounts in horse sera have been performed using .’s (1965) immunodiffusion technique. Relative values against a chosen standard of 100 % were determined for a total of 435 horses. There was considerable variation between horses, the highest Pr value being 125 and the lowest 50 % of the standard. In animals of the same Pr phenotype the mean Pr values were significantly higher (P < 0.001) in foals than in mares. In Norwegian Trotter horses the Pr value of Pr NN animals was significantly higher than that of Pr SS phenotypes, whereas the mean Pr values of Pr SS was sig...
Concentration of serum prealbumin (PR) protein in sick horses and its correlation to blood leucocyte count and albumin content in serum.
Acta veterinaria Scandinavica    January 1, 1980   Volume 21, Issue 4 482-497 doi: 10.1186/BF03546836
Ek N.Studies of Pr protein concentrations in sera of sick horses were carried out using ’s (1965) immunodiffusion technique. Relative values against a chosen standard of 100 were determined for a total of 102 horses. Horses with acute infections had Pr protein values significantly above the normal. The highest individual Pr protein value recorded in this group was 202. Horses suffering from acute laminitis and malignant tumours also had increased Pr protein values. There was a positive correlation between the Pr protein value and the blood leucocyte count and a negative correlation between the P...
Topographic antigenic determinants on cytochrome c. Immunoadsorbent separation of the rabbit antibody populations directed against horse cytochrome.
The Journal of biological chemistry    December 25, 1979   Volume 254, Issue 24 12706-12716 
Jemmerson R, Margoliash E.Seven populations of site-specific antibodies were isolated from each of three sera of rabbits immunized against glutaraldehyde-polymerized horse cytochrome c. The antibodies were separated using an immunoadsorption scheme which employed the following cytochromes c: horse, beef, guanaco, rabbit, mouse testicular, pigeon, and the cyanogen-bromide cleaved fragment of the rabbit protein containing residues 1 to 65. The monovalent, antigen-binding fragments of the antibodies (Fab') gave 1:1 stoichiometries with native horse cytochrome c in fluorescence quenching assays. Cross-reactivities with het...
Comparison of yeast and beef cytochrome c oxidases. Kinetics and binding of horse, fungal, and Euglena cytochromes c.
The Journal of biological chemistry    December 10, 1979   Volume 254, Issue 23 11973-11981 
Dethmers JK, Ferguson-Miller S, Margoliash E.No abstract available
Identification of a protein component of horse kidney brush border D-glucose transport system.
Biochemical and biophysical research communications    October 29, 1979   Volume 90, Issue 4 1387-1392 doi: 10.1016/0006-291x(79)91189-6
Poiree JC, Mengual R, Sudaka P.No abstract available
[Protein and enzymatic activity levels of the synovial fluid in the horse].
Schweizer Archiv fur Tierheilkunde    October 1, 1979   Volume 121, Issue 10 521-531 
Poncet PA, Gerber H, Tschudi P, Diehl M.No abstract available
Identification of alpha1-lipoproteins in crossed immunoelectrophoresis.
Clinical chemistry    October 1, 1979   Volume 25, Issue 10 1749-1756 
Cline LJ, Crowle AJ.Evans Blue dye binds selectively, but with different avidities, to five major antigens in human serum. The anodic mobility of the antigen-dye complexes is greater than that of the antigens alone in crossed immunoelectrophoresis, which is of practical value for identification. We used this characteristic to show that in some human sera there is a population of alpha1-lipoprotein molecules that migrates electrophoretically in the beta-lipoprotein region, where in conventional zone electrophoresis it could be mistaken for beta-lipoprotein. We also demonstrate that horses, unlike rabbits, rarely m...
Isolation and partial characterization of prolactin from equine pituitary gland (hypophysis).
American journal of veterinary research    September 1, 1979   Volume 40, Issue 9 1303-1306 
Chen CL, Neilson JT, Kumar MS, Estes KS.Highly purified equine prolactin was prepared from equine pituitary glands (hypophysis) by serial extractions with water at pH 5.5, 0.1 M (NH4)2SO4 at pH 4.0, and 0.25 M (NH4)2SO4 at pH 5.5 to remove other hormones, and then finally with 70% ethanol at pH 9.3 to 10.0 to extract prolactin. Preliminary purification of the extract involved salting out other substances with 0.1% NaCl at pH 9.0. Prolactin was precipitated out by adding three times the volume of 95% ethanol at 4 C. This prolactin preparation had a biological potency of 24 IU/mg. Further purification by isoelectric focusing on a pH g...
Gel filtration analysis of equine ferritin subunits.
FEBS letters    August 1, 1979   Volume 104, Issue 1 51-54 doi: 10.1016/0014-5793(79)81083-2
Arosio P.No abstract available
Energy and protein under-nutrition in the weanling filly foal.
The British veterinary journal    July 1, 1979   Volume 135, Issue 4 331-337 doi: 10.1016/s0007-1935(17)32835-x
Ellis RN, Lawrence TL.No abstract available
Identification and characterisation of the major antiproteases in equine serum and an investigation of their role in the onset of chronic obstructive pulmonary disease (COPD).
Equine veterinary journal    July 1, 1979   Volume 11, Issue 3 177-182 doi: 10.1111/j.2042-3306.1979.tb01336.x
Matthews AG.Three major antiprotease components in equine serum were identified and characterised. These were the acidic prealbumin Pr, the homologue of human alpha-1 antitrypsin and 2 protease binding proteins, the acidic prealbumin Xc and alpha-2 macroglobulin, both capable of inhibiting the proteolytic activity of trypsin, but with only limited inhibitory effect on its esterolytic activity. The possible role of these serum antiproteases in the onset of chronic obstructive pulmonary disease (COPD), analogous to the hereditary dysproteinaemia of alpha-1 antitrypsin in man, was investigated. There was no ...
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