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.
Horse pancreatic colipase: isolation by a detergent method and amino terminal sequence of the polypeptide chain.
Biochimie    January 1, 1978   Volume 60, Issue 1 103-107 doi: 10.1016/s0300-9084(78)80207-7
Julien R, Rathelot J, Canioni P, Sarda L, Gregoire J, Rochat H.No abstract available
Response to dietary nitrogen in ponies.
Equine veterinary journal    January 1, 1978   Volume 10, Issue 1 65-68 doi: 10.1111/j.2042-3306.1978.tb02219.x
Reitnour CM.Utilisation of nitrogen was studied in 4 crossbred ponies. A latin square design was used to study the effects of corn gluten meal, casein or urea when added to a low protein basal diet. Apparent nitrogen digestion, nitrogen retention, total plasma protein, plasma urea and plasma-free amino acids were measured. The addition of corn gluten meal, casein or urea to the basal ration increased apparent digestion of nitrogen. Casein produced a significantly greater (P less than 0.05) nitrogen retention than corn gluten meal or urea. Plasma urea nitrogen increased significantly (P less than 0.01) in ...
Polymorphic post-albumin of cattle and horse plasma identified as vitamin D binding protein (Gc protein).
Animal blood groups and biochemical genetics    January 1, 1978   Volume 9, Issue 1 37-40 doi: 10.1111/j.1365-2052.1978.tb01409.x
Gahne B, Juneja RK.Cattle and horse plasma samples of known post-albumin types were radiolabelled with 14C-vitamin D3. These samples were then analysed by polyacrylamide gel electrophoresis, followed by autoradiography. The patterns observed were identical to those of post-albumin variants. The polymorphic post-albumin protein of cattle and horse was thus identified as the vitamin D binding protein and homologous to the Gc protein of human plasma.
Genetic polymorphism of the vitamin D binding protein and another post-albumin protein in horse serum.
Animal blood groups and biochemical genetics    January 1, 1978   Volume 9, Issue 1 29-36 doi: 10.1111/j.1365-2052.1978.tb01408.x
Juneja RK, Gahne B, Sandberg K.Horizontal polyacrylamide gel electrophoreses, on 10% separation gel, of horse serum revealed polymorphism of the vitamin D binding protein (Gc protein) and another post-albumin protein (Pa). Family data supported the hypothesis that Gc and Pa types were controlled by autosomal codominant alleles. For both Gc and Pa proteins, the homozygous types showed a single fraction while the heterozygous type had two fractions. Pa types were found to be identical to the post-albumin types reported earlier by starch gel electrophoresis. Two Gc alleles, GcF and GcS, and three Pa alleles, Pa D, Pa F and Pa ...
Analysis of a complex antigenic site on horse cytochrome c.
Advances in experimental medicine and biology    January 1, 1978   Volume 98 119-129 doi: 10.1007/978-1-4615-8858-0_6
Jemmerson R, Margoliash E.Of the antigenic determinants so far identified for cytochrome c, only one involves more than a single amino acid substitution between the immunogen and host proteins. Both a threonine at position 89 and a glutamic acid at position 92 control one of the three antigenic sites identified in horse cytochrome c, as expressed in rabbits. Three antibody subpopulations, all directed against this region of the molecule, were isolated from the serum of a single rabbit by adsorption on a series of insolubilized cytochromes c. Antibody fluorescence quenching titrations with a variety of cytochromes c wer...
Somatostatin-containing cells in the rat and horse pancreatic islets.
The Tohoku journal of experimental medicine    January 1, 1978   Volume 124, Issue 1 57-64 doi: 10.1620/tjem.124.57
Ito S, Yamada Y, Hayashi M, Matsubara Y.Somatostatin-, glucagon- and insulin-containing cells in the rat and horse pancreatic islets were investigated by an indirect immunofluorescent technique using antibodies to insulin, glucagon and somatostatin. In the rat pancreatic islets, insulin-containing cells were located centrally, and glucagon and somatostatin or somatostatin-like substance (SLS)-containing cells were peripherally disposed and glucagon-containing cells were situated more peripherally as compared with distribution of somatostatin-containing cells. On the other hand, in the horse pancreatic islets, insulin-containing cell...
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c.
The Journal of biological chemistry    November 10, 1977   Volume 252, Issue 21 7743-7751 
Osheroff N, Feinberg BA, Margoliash E, Morrison M.Iodination of horse cytochrome c with the lactoperoxidase-hydrogen peroxide-iodide system results initially in the formation of the monoiodotyrosyl 74 derivative. This singly modified protein was obtained in pure form by ion exchange chromatography and preparative column electrophoresis. It shows an intact 695 nm absorption band, the midpoint potential of the native protein, a nuclear magnetic resonance spectrum which indicates an undisturbed heme crevice structure, a normal reaction with antibodies directed against native horse cytochrome c, and circular dichroic spectra in which the only cha...
A subunit-sized butyrylcholinesterase present in high concentrations in pooled rabbit serum.
The Biochemical journal    November 1, 1977   Volume 167, Issue 2 367-376 doi: 10.1042/bj1670367
Main AR, McKnelly SC, Burgess-Miller SK.A butyrylcholinesterase of mol.wt. approx. 83000 was observed in pooled rabbit serum. The enzyme was named monomeric butyrylcholinesterase to distinguish it from the larger oligomeric butyrylcholinesterase of horse and human serum whose subunits are the same size as the monomeric enzyme. The active-site concentration of monomeric butyrylcholinesterase in the pooled serum was 0.18mum, which is five times the concentration of butyrylcholinesterase in pooled horse serum. This was surprising, since the horse serum is regarded as a rich source of butyrylcholinesterase, whereas rabbit serum is not g...
Circular dichroism of porcine, bovine, and equine pancreatic phospholipases A2 and their zymogens. Unusual conformations simulating helix content.
Biochimica et biophysica acta    October 26, 1977   Volume 494, Issue 2 285-292 doi: 10.1016/0005-2795(77)90157-x
Jirgensons B, de Haas GH.Conformation of porcine, bovine, and equine pancreatic phospholipases A2 (EC 3.1.1.4) and their zymogens was studied by the circular dichroism (CD) probe in the far and near ultraviolet spectral zones. All these phospholipases and their zymogens displayed CD curves suggesting the presence of moderate amounts of α-helical conformation. However, on the basis of known primary structure and recent X-ray structural analysis of prophospholipase A2 crystals (Drenth, J., Enzing, C.M., Kalk, K.H. and Vessies, J.C.A. (1976) Nature 264, 373–377), it has to be concluded that the positive CD band cen...
Semisynthetic cytochrome c.
Proceedings of the National Academy of Sciences of the United States of America    October 1, 1977   Volume 74, Issue 10 4248-4250 doi: 10.1073/pnas.74.10.4248
Barstow LE, Young RS, Yakali E, Sharp JJ, O'Brien JC, Berman PW, Harbury HA.Horse heart cytochrome c can be split with cyanogen bromide into a heme peptide (residues 1-65) and a nonheme peptide (residues 66-104). In a process involving (i) complex formation between the two fragments and (ii) restoration of the severed peptide linkage, a fully active cytochrome c preparation can be re-formed. Use has been made of this process to couple the heme peptide to peptide 66-104 synthesized by the Merrifield solid-phase procedure. The semisynthetic product formed in this manner is indistinguishable from reconstituted cytochrome c prepared with nonsynthetic peptide 66-104.
Phylogeny of the neurophysins: complete amino acid sequence of horse MSEL-neurophysin.
FEBS letters    August 15, 1977   Volume 80, Issue 2 374-376 doi: 10.1016/0014-5793(77)80479-1
Chauvet MT, Codogno P, Chauvet J, Acher R.No abstract available
The structure of horse methaemoglobin at 2-0 A resolution.
Journal of molecular biology    August 15, 1977   Volume 114, Issue 3 385-414 doi: 10.1016/0022-2836(77)90256-x
Ladner RC, Heidner EJ, Perutz MF.No abstract available
Characterization of a retravirus isolated from squirrel monkeys.
Journal of virology    August 1, 1977   Volume 23, Issue 2 384-393 doi: 10.1128/JVI.23.2.384-393.1977
Schochetman G, Fine D, Arthur L, Gilden R, Heberling R.A new retravirus (SMRV) isolated from a squirrel monkey, Saimiri sciureus, has an Mg2+-dependen reverse transcriptase and a buoyant density of 1.17 g/cm3 in sucrose and 1.21 g/cm3 in cesium chloride, similar to the mouse mammary tumor virus and the Mason-Pfizer monkey virus. The polypeptide patter of SMRV as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was distinct from the reported polypeptide patterns of known retraviruses. Four major polypeptides of molecular weights 40,000, 20,000, 14,000 and 8,000 were resolved in virus propagated in human, mink, and canine cell...
The oxidation of ferrocytochrome c in nonbinding buffer.
Canadian journal of biochemistry    August 1, 1977   Volume 55, Issue 8 796-803 doi: 10.1139/o77-118
Peterman BF, Morton RA.The apparent equilibrium constant and rate of oxidation was investigated for the reaction of cytochrome c with iron hexacyanide. It was found that if horse heart ferricytochrome c was exposed to ferricyanide (to oxidize traces of reduced protein) the cytochrome subsequently, even after extensive dialysis, had an apparent equilibrium constant different from that of electrodialyzed protein. The effect of ferricyanide ion apparently cannot be removed by ordinary dialysis. The ionic strength dependence of the apparent equilibrium constant and bimolecular oxidation rate constant was measured in the...
Electron-transfer protein reactivities. Kinetic studies of the oxidation of horse heart cytochrome c, Chromatium vinosum high potential iron-sulfur protein, Pseudomonas aeruginosa azurin, bean plastocyanin, and Rhus vernicifera stellacyanin by pentaamminepyridineruthenium(III).
Journal of the American Chemical Society    July 20, 1977   Volume 99, Issue 15 5158-5167 doi: 10.1021/ja00457a042
Cummins D, Gray HB.No abstract available
Electronic and steric factors affecting ligand binding: horse hemoglobins containing 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme.
The Journal of biological chemistry    June 25, 1977   Volume 252, Issue 12 4225-4231 
Seybert DW, Moffat K, Gibson QH, Chang CK.Horse globin has been recombined with 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme to yield the corresponding reconstituted hemoglobins, and the ligand binding reactions of these reconstituted hemoglobins have been examined in detail. Both hemoglobins exhibit relatively high n values, but 2,4-dimethyldeuterohemoglobin displays a consistently higher oxygen affinity than native hemoglobin, whereas the oxygen affinity of 2,4-dibromodeuterohemoglobin is consistently lower than that of native hemoglobin. The rate constants l’, and 1’4 for the binding of the first and fourth molecules of C...
Equine angiotensin converting enzyme: a zinc metalloenzyme.
Clinical and experimental pharmacology & physiology    May 1, 1977   Volume 4, Issue 3 267-281 doi: 10.1111/j.1440-1681.1977.tb02624.x
Fernley RT.1. Angiotensin I converting enzyme from horse plasma has been extensively purified and shown to be homogeneous by disc-gel electrophoresis. 2. The metal ion involved in the catalytic reaction of the enzyme has been identified for the first time as zinc by atomic absorption spectrometry. 3. A number of other physicochemical properties of the enzyme are described and compared with results obtained by other investigators. The molecular weight was determined by gel filtration to be 113 000 daltons. The pH maximum was found to be 7-4. The chloride activation of the enzyme appears to act by facilita...
Studies on the synovia in healthy horses with particular reference to the protein composition.
Equine veterinary journal    April 1, 1977   Volume 9, Issue 2 87-91 doi: 10.1111/j.2042-3306.1977.tb03990.x
Liberg P, Magnusson LE, Schougaard H.Synovial fluid and blood were collected from 18 clinically healthy brood mares in resting conidition. The following parameters were analysed: total leucocytes, glucose, alkaline phosphatase (AP), lactate dehydrogenase (LDH), total protein, albumin, total globulin, albumin/globulin ratio and electrophoretic protein picture. The serum/synovia ratios were calculated for all parameters. It was considered to be of greater diagnostic value to compare these serum/synovia ratios rather than to look at the individual concentrations in synovia. The results obtained did not materially differ from those i...
Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice.
Biochimica et biophysica acta    March 28, 1977   Volume 491, Issue 1 265-274 doi: 10.1016/0005-2795(77)90062-9
Evenberg A, Meyer H, Verheij HM, de Haas GH.Two phospholipases A2 (EC 3.1.1.4) with different isoelectric points have been isolated from horse pancreas in high yield (880 mg/kg tissue). From pancreatic juice the more acidic species was isolated as the sole phospholipase A2. Upon tryptic activation the zymogens release a hepta- and pentapeptide, respectively from the N-terminal part of the protein giving rise to the formation of one single enzyme with a specific activity higher than that of pancreatic phospholipases A2 from other mammalian species. Horse phospholipase A2 differs from the porcine and bovine enzymes with respect to amino a...
Amino acid sequence of phospholipase A2 from horse pancreas.
The Journal of biological chemistry    February 25, 1977   Volume 252, Issue 4 1189-1196 
Evenberg A, Meyer H, Gaastra W, Verheij HM, De Haas GH.The complete amino acid sequence of phosphlipase A2 (EC 3.1.1.4) from horse pancreas was determined. The protein controls of a single polypeptide chain of 125 amino acids and has a molecular weight of 13,927. The chain is crosslinked by seven disulfide bridges. The sequence was determined by automated Edman degradation of the intact protein and several of the large peptide fragments. Smaller peptides were analyzed by manual Edman degradation. Fragmentation of the peptide chain was accomplished by enzymatic digestion with trypsin, chymotrypsin, and thermolysin. The final overlap was found by di...
Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase.
The Journal of biological chemistry    February 10, 1977   Volume 252, Issue 3 919-926 
Kang CH, Ferguson-Miller S, Margoliash E.1. The steady state kinetics for the oxidation of ferrocytochrome c by yeast cytochrome c peroxidase are biphasic under most conditions. The same biphasic kinetics were observed for yeast iso-1, yeast iso-2, horse, tuna, and cicada cytochromes c. On changing ionic strength, buffer anions, and pH, the apparent Km values for the initial phase (Km1) varied relatively little while the corresponding apparent maximal velocities varied over a much larger range. 2. The highest apparent Vmax1 for horse cytochrome c is attained at relatively low pH (congruent to 6.0) and low ionic strength (congruent to...
Guanidination of horse methemoglobin.
Archives of biochemistry and biophysics    February 1, 1977   Volume 179, Issue 1 322-327 doi: 10.1016/0003-9861(77)90117-5
Sakura JD, Rupley JA.Reaction of horse methemoglobin with O-methylisourea at pH 10.2 results in 95% conversion of lysine residues to homoarginine. Analysis of the chymotryptic peptides showed that no single ϵ-amino group was unreactive. Guanidination decreases the dependence of the sedimentation coefficient on hydrogen ion concentration in the range of pH 8 to 11 and did not affect the dependence on protein concentration at pH 7. These results support the conclusion that the lysine side chains involved in subunit contacts have sufficient freedom to accommodate the small changes in bulk and geometry associated wit...
Heterogeneity in whey proteins of mare’s milk.
Journal of dairy science    February 1, 1977   Volume 60, Issue 2 274-277 doi: 10.3168/jds.S0022-0302(77)83864-2
Kingsbury ET, Gaunt SN.The possible existence of multiple forms in the whey proteins of mare's milk was investigated. When individual milk samples from over 300 animals of various breeds were examined, four forms of an undescribed whey protein could be observed. Based on chemical properties and electrophoretic behavior, this protein has been identified tentatively as Whey1 (Wh1). A single case of heterogeneity in mare's alpha-lactalbumin also was observed. Previously described variation in beta-lactoglobulin could not be confirmed. The results of this study provide further evidence of the widespread, perhaps univers...
Serum enzyme and protein concentrations in English shire horses.
The Veterinary record    January 29, 1977   Volume 100, Issue 5 91-92 doi: 10.1136/vr.100.5.91
Blackmore DJ, Kent JE.No abstract available
Amino acid composition of casein isolated from the milks of different species.
Canadian journal of zoology    January 1, 1977   Volume 55, Issue 1 231-236 doi: 10.1139/z77-026
Lauer BH, Baker BE.Casein was isolated from the milks of the following species: cow, horse, pig, reindeer, caribou, moose, harp seal, musk-ox, polar bear, dall sheep, and fin whale. The caseins were subjected to acid hydrolysis, the resultant amino acids were converted to their n-butyl-N-trifluoroacetyl esters, and the amino acid composition of the caseins was determined by gas chromatographic analysis of these esters. Notable among the results was the close similarity, with respect to amino acid composition, of reindeer and caribou caseins. The results of the amino acid analyses of the other caseins are present...
Relationship of protein concentration and water content of equine serum and plasma samples.
Veterinary clinical pathology    January 1, 1977   Volume 6, Issue 3 18-20 doi: 10.1111/j.1939-165x.1977.tb00771.x
Carlson GP, Harrold DR.A highly significant correlation between the water content and protein concentration of equine serum and plasma samples was demonstrated over a wide range of concentrations. A close correlation was also observed between protein concentration as estimated by refractometry and as determined by the biuret procedure for equine serum and plasma samples.
Studies on cytochrome C. XIII. Synthesis of the protected undecapeptide (sequence 77-87) of horse heart cytochrome c.
International journal of peptide and protein research    January 1, 1977   Volume 10, Issue 2 89-94 
Borin G, Filippi B, Stivanello D, Marchiori F.A solution synthesis of Z-Gly-Thr-Lys (Tfa)-Met-Ile-Phe-Ala-Gly-Ile-Lys (Tfa)-Lys (Tfa)-NHNH-Boc corresponding to the sequence 77-87 of horse heart cytochrome c is described. The protected undecapeptide was obtained from intermediate hepta- and tetrapeptide fragments by an azide coupling.
Rapid heterolysis of indophenyl acetate by a constituent of a preparation of horse serum cholinesterase.
Enzyme    January 1, 1977   Volume 22, Issue 2 130-136 doi: 10.1159/000458777
Hubbard CD, Shoupe TS.A transient phase for the hydrolysis of indophenyl acetate by the commercial preparation of horse serum cholinesterase was observed on a stopped-flow spectrophotometer. It was found that the transient process is a reaction of the ester with a major component of the preparation and is not caused by the serum cholinesterase enzyme. This noncholinesterase component was isolated and the dependence of its concentration and that of the ester upon the transient liberation of the indophenolate ion were determined. Studies with the isolated component and subsequent analyses have led to the tentative id...
Identification of the PR prealbumin proteins in horse serum.
Acta veterinaria Scandinavica    January 1, 1977   Volume 18, Issue 4 458-470 doi: 10.1186/BF03548409
Ek N.The Pr protein, which is one of the major equine acidic prealbumins and which consists of a large number of phenotypes, has been studied with regard to its chemical identity. Serum samples of known Pr phenotype which had been treated with varying amounts of bovine trypsin were subjected to starch gel electrophoresis at pH 4.8. When a certain amount of trypsin was used, the Pr protein was markedly affected, whereas the other acidic prealbumins retained their normal electrophoreitic pattern. Extracts from three different regions of the acidic prealbumin field were tested by the casein precipitat...
Proton-dependent dissociation equilibrium of hemoglobin. 1. A 700-nanometer light-scattering study on horse methemoglobin in the pH range 4.8 to 7.2.
Biochemistry    December 28, 1976   Volume 15, Issue 26 5693-5697 doi: 10.1021/bi00671a002
Schroeder E, Wollmer A, Kubicki J, Ohlenbusch HD.The effect of proton concentration upon the subunit dissociation of horse methemoglobin has been investigated at two ionic strengths by light scattering photometry at 700 nm. Differential refractometry revealed a slight but systematic decrease of the specific refractive index increment with decreasing protein concentration for solutions in dialytic equilibrium with the solvent. In the pH range 4.8-7.2 the dissociation can be described by a simple equilibrium between tetramers and dimers. The dissociation constant Kd of the met derivative is found to be very similar to those of the O2- and CO-l...
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