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.
Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme.
European journal of biochemistry    March 15, 1988   Volume 172, Issue 3 527-533 doi: 10.1111/j.1432-1033.1988.tb13920.x
Johansson J, von Bahr-Lindström H, Jeck R, Woenckhaus C, Jörnvall H.The primary structure of the mitochondrial form of horse liver aldehyde dehydrogenase has been determined, utilizing peptide analyses and homology with other enzyme forms. The subunit exhibits N-terminal heterogeneity in size similar to that for the corresponding human mitochondrial protein, the longest form having 500 residues. Catalase was identified as a contaminant of the preparations. All four pairs within a set of aldehyde dehydrogenases can now be compared, including the same two species variants (horse and human) for both the cytosolic and mitochondrial enzyme, revealing characteristic...
Pharmacokinetics of sodium amoxicillin in horses.
Research in veterinary science    March 1, 1988   Volume 44, Issue 2 233-236 
Montesissa C, Carli S, Sonzogni O, Garlappi R.The pharmacokinetics of sodium amoxicillin were investigated after intravenous and intramuscular administration of a single dose of 15 mg kg-1 body-weight to five horses. A rapid distribution phase was noted after intravenous administration (t1/2 alpha about 20 minutes). The t1/2 beta values obtained after the intravenous and the intramuscular administration were significantly different (P less than 0.05). The bioavailability obtained was about 67 per cent. Plasma protein binding, evaluated in vitro, showed that the percentage of bound fraction was 37 to 38 per cent. It was concluded that sodi...
Microanalysis of the amino-acid sequence of monomeric beta-lactoglobulin I from donkey (Equus asinus) milk. The primary structure and its homology with a superfamily of hydrophobic molecule transporters.
Biological chemistry Hoppe-Seyler    March 1, 1988   Volume 369, Issue 3 171-179 doi: 10.1515/bchm3.1988.369.1.171
Godovac-Zimmermann J, Conti A, James L, Napolitano L.The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric beta-lactoglobulin of type I. With the inclusion of donkey beta-lactoglobulin I there are 13% common residues amongst the members of the beta-lactoglobulin family. Donkey beta-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporters. A rapid method for peptide i...
[Sublimation-dried mare’s milk and the possibility of its use in creating infant and dietary food products].
Voprosy pitaniia    March 1, 1988   Issue 2 64-67 
Stoianova LG, Abramova LA, Ladodo KS.The main biological parameters were studied in sublimated mare's milk: protein fraction composition, amino-acid spectrum, fatty-acid composition of lipids and the content of vitamins and mineral substances. A high biological value of the sublimated mare's milk has been proved, as well as significant proximity of its composition to human milk. Preliminary data have evidenced expediency of mare's milk use for the development of adapted milk mixtures for baby foods. However, the fatty component of the mixtures needs certain correction by addition of vegetable oil. The sublimated mare's milk can b...
Histological evaluation of wound healing in horses treated with the protein-free hemodialysate Solcoseryl and its hexosylceramide fraction.
Zentralblatt fur Veterinarmedizin. Reihe B. Journal of veterinary medicine. Series B    February 1, 1988   Volume 35, Issue 2 84-95 doi: 10.1111/j.1439-0450.1988.tb00472.x
Liebich HG, Hamm D, Jöchle W.No abstract available
Nitrogen metabolism in mature horses at varying levels of work.
Journal of animal science    February 1, 1988   Volume 66, Issue 2 407-412 doi: 10.2527/jas1988.662407x
Freeman DW, Potter GD, Schelling GT, Kreider JL.Nitrogen metabolism was measured in five mature geldings performing varying levels of work that simulated race training. Following an initial maintenance period without forced exercise, workload was increased in succeeding 18-d periods by doubling the distance the horses were galloped in each period from period 2 through 4. A 4-d N balance experiment was conducted at the end of each 18-d period. The maximum distance galloped daily, which was in period 4, was repeated in period 5. Then, workloads were decreased through period 7. Nitrogen balance was determined in two additional periods, 8 and 9...
Interspecies variation in milk composition among horses, zebras and asses (Perissodactyla: Equidae).
The Journal of dairy research    February 1, 1988   Volume 55, Issue 1 57-66 doi: 10.1017/s0022029900025851
Oftedal OT, Jenness R.Milk samples of four species of wild equids (onager, Equus hemionus onager; mountain zebra, E. zebra hartmannae; plains zebra, E. burchelli; Przewalski horse, E. caballus przewalskii) and two domesticated equids (ass, E. asinus; pony, E. caballus) were analysed. At mid to late lactation the milks of all species were very similar, containing on average 10-12% total solids, 1-2% fat, 1.6-1.8% true protein, 6-7% 'lactose', 0.3-0.5% ash, 0.08-0.12% calcium, 0.04-0.07% phosphorus and a calculated energy content of 2.0-2.4 kJ/g. Milk samples collected in the first 2 weeks after birth showed elevated...
Digestion of hay protein in different segments of the equine digestive tract.
Journal of animal science    February 1, 1988   Volume 66, Issue 2 400-406 doi: 10.2527/jas1988.662400x
Gibbs PG, Potter GD, Schelling GT, Kreider JL, Boyd CL.Mature ponies fitted with permanent ileal cannulas were used in a 3 X 3 Latin square experiment to quantify prececal, postileal and total tract digestion of hay protein. Coastal Bermuda grass (CB), containing 11.7% crude protein, and two qualities of alfalfa, containing 15.0% (low-protein alfalfa; LA) and 18.1% (high-protein alfalfa; HA) crude protein, were fed in coarsely chopped form at 2% of body weight daily. Total tract apparent digestibility of the N in HA (73.8%) was higher than that in CB (57.0%; P less than .05) and was slightly higher than that in LA (66.1%; P less than .10). Nitroge...
The characterization of equine herpes virus-1-infected cell polypeptides recognized by equine lymphocytes.
Immunology    February 1, 1988   Volume 63, Issue 2 193-198 
Bridges CG, Ledger N, Edington N.Ponies, without evidence of previous exposure to Equine herpes virus-1 (EHV-1), were experimentally infected with EHV-1 subtype 2 and investigated for lymphocyte transformation to virus-infected cell polypeptides, as shown by separation with gel electrophoresis. Animals made significant responses to Western blot fractions that corresponded to molecular weights of approximately 30,000, 40,000-45,000, 60,000-65,000, 80,000-95,000 and 100,000-140,000 MW. These molecular weight ranges correlated with the positions of major EHV-1 subtype 2 glycoproteins that were found at migration distances approx...
Noncatalytic protein component of elastase from horse leucocytes. A protein with regulatory function.
The International journal of biochemistry    January 1, 1988   Volume 20, Issue 1 105-108 doi: 10.1016/0020-711x(88)90019-5
Potempa J, Korzus E, Silberring J, Dubin A.1. Noncatalytic protein component (NPC), a strongly acidic protein (pH = 4.5) was separated from native horse leucocyte elastase 1. 2. This protein reduces elastinolytic properties of elastases: 1 and 2A probably by decreasing their isoelectric points. 3. A possible regulatory role of this protein may be inferred from a higher affinity of elastase 1 to NPC rather than to elastin.
The homology between the serum proteins PO2 in pig, Xk in horse and alpha 1B-glycoprotein in human.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1988   Volume 90, Issue 4 751-756 doi: 10.1016/0305-0491(88)90330-6
Van de Weghe A, Coppieters W, Bauw G, Vandekerckhove J, Bouquet Y.1. Pig serum Po2 protein and horse Xk protein were purified by FPLC, non-denaturing 2D agarose-PAGE and 2D IPG-PAGE. 2. The separated fractions were electroblotted to poly(4-vinyl-N-methylpyridinium iodide) coated GF/C glass fiber sheets. 3. The partial amino acid sequences and amino acid compositions of different genetic variants of the proteins were determined. 4. The results proved that previously reported polymorphic serum post-albumins in each of these species were homologous to human plasma alpha 1B-glycoprotein.
Comparative immunochemical studies of carbonic anhydrase III in horses and other mammalian species.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1988   Volume 91, Issue 1 91-96 doi: 10.1016/0305-0491(88)90118-6
Nishita T, Matsushita H.1. Carbonic anhydrase III (CA-III) from different mammalian species (horse, cow, dog, cat, rat and rabbit) has been analyzed by the immunodiffusion technique with anti-equine CA-III serum. 2. Immunodiffusion demonstrated the absence of cross-reactivity between isozyme CA-I, CA-II, and CA-III. 3. Cross-reactions were observed between the CA-III from all the species examined except the rabbit. 4. Molecular weights and isoelectric points of CA-III from different species were determined by Western blotting.
Heparan sulfate proteoglycan from human and equine glomeruli and tubules.
The International journal of biochemistry    January 1, 1988   Volume 20, Issue 12 1391-1400 doi: 10.1016/s0020-711x(98)90007-6
van den Heuvel LP, Veerkamp JH, Monnens LA, Schröder CH.1. Proteoglycans were isolated from human and equine glomeruli or tubules by guanidine extraction and anion exchange chromatography. 2. These proteoglycan preparations contained about equal amounts of heparan sulfate and chondroitin sulfates. 3. During the preparation of glomerular or tubular basement membranes the main part of proteoglycans (greater than 50%) was extracted in the salt extract. Chondroitin sulfate proteoglycan was mainly found in the water and salt extracts of glomeruli and tubules, heparan sulfate proteoglycan in the deoxycholate extracts and the basement membranes. 4. The gl...
Structural aspects of the plasminogen of various species.
Enzyme    January 1, 1988   Volume 40, Issue 2-3 63-69 doi: 10.1159/000469147
Schaller J, Rickli EE.The N-terminal amino acid sequence of equine, ovine, canine, goat and rabbit plasminogen were determined and compared with those already known of the human, bovine, porcine and feline molecule. Furthermore, the kringle 4 domains of equine, ovine, canine and goat plasminogen, prepared by limited cleavage with elastase, were sequenced and compared with the known species of human, bovine, porcine and chicken plasminogen. Homology with the human kringle 4 ranges between 73% (chicken) and 90% (bovine). Comparison of sequences, fragmentation patterns with elastase and adsorption on lysine-Bio-Gel su...
Structural, histochemical and biochemical observations on horse milk-fat-globule membranes and casein micelles.
Histochemistry    January 1, 1988   Volume 88, Issue 3-6 357-365 doi: 10.1007/BF00570295
Welsch U, Buchheim W, Schumacher U, Schinko I, Patton S.Horse milk fat globules (MFGs) and casein micelles were studied using freeze fracturing, freeze etching and thin-section electron microscopy, as well as lectin histochemistry, gel electrophoresis, and Western blotting. Horse MFGs were found to be relatively small, their average volume-surface diameter being about 2.75 microns. The MFG membrane is composed of three layers: an inner proteinaceous coat occasionally having a paracrystalline substructure, a unit membrane, and a prominent filamentous glycocalyx. The last is rich in glycoconjugates, as revealed by its binding of various lectins. In a...
Characterization of a homogeneous paraprotein from a horse with spontaneous multiple myeloma syndrome.
Veterinary immunology and immunopathology    December 1, 1987   Volume 17, Issue 1-4 69-77 doi: 10.1016/0165-2427(87)90128-0
Seide RK, Jacobs RM, Dobblestein TN, Kehoe JM.A novel myeloma paraprotein has been isolated from a horse with a lymphoid tumor. The protein was a euglobulin and consequently was readily isolated from serum in pure form and high yield by simple dilution in distilled water. The purified intact protein had a molecular weight of 150,000 and was composed of heavy and light chains, both of which had blocked amino-termini and were thus not susceptible to amino-terminal sequence analysis. The amino acid compositions of these respective chains corresponded to those of comparable chains from immunoglobulins of other species. Peptide maps of parapro...
The major protamine from stallion sperm. Isolation and amino-acid sequence.
Biological chemistry Hoppe-Seyler    December 1, 1987   Volume 368, Issue 12 1619-1626 doi: 10.1515/bchm3.1987.368.2.1619
Ammer H, Henschen A.The major stallion protamine was isolated from sperm cell nuclei by extraction with 6M guanidine/5% mercaptoethanol, alkylation with 4-vinylpyridine and subsequent reversed-phase high-performance liquid chromatography. The primary structure of stallion protamine was determined by N-terminal sequencing of the intact protein and of the fragments obtained from thermolysin cleavage of the S-pyridylethylated and from endoproteinase Lys-C cleavage of the S-aminoethylated protein. Stallion protamine consists of 49 amino-acid residues and shows 49% identity with all other sequenced mammalian type 1 pr...
[Isolation and purification of proteolytic enzymes on organo-silica sorbents with immobilized gramicidin S].
Ukrainskii biokhimicheskii zhurnal (1978)    November 1, 1987   Volume 59, Issue 6 28-33 
Ignatchenko AP, Bogomaz VI, Tugaĭ VA, Chuĭko AA.Biospecific sorbents for affinity chromatography of proteolytic enzymes have been synthesized by attaching cyclopeptide antibiotic gramicidin S to organo-silica supports. It is shown possible to attach gramicidin S to the organo-silica supports using glutaric aldehyde, p-benzoquinone, soluble and insoluble carbodiimides. The sorbents prepared by these methods were successfully applied for the purification of the crude pepsin from horse gastric juice and proteolytic complex produced by Acremonium chrysogenum.
Immunocytochemical localisation of carbonic anhydrase isozyme III in equine skeletal muscle.
Equine veterinary journal    November 1, 1987   Volume 19, Issue 6 509-513 doi: 10.1111/j.2042-3306.1987.tb02660.x
Nishita T, Matsushita H, Kai M.The location of carbonic anhydrase III (CA-III) in frozen sections of biopsies of Thoroughbred horse skeletal muscle was studied. Fibre types were determined by ATP-ase and succinate dehydrogenase staining. CA-III isozyme was detected using a peroxidase conjugated anti-CA-III antibody. CA-III was found to be localised in slow twitch oxidative fibres (ST), but was also present in fast twitch oxidative (FTH) fibres in small amounts. Fast twitch glycolytic (FT) fibres were stained lightly compared with control sections. The concentrations of CA-III in muscle and liver were 70 micrograms/mg protei...
Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: a fluorescence quenching study on the ionic strength dependence of the interaction.
Archives of biochemistry and biophysics    November 1, 1987   Volume 258, Issue 2 621-629 doi: 10.1016/0003-9861(87)90385-7
Vitello LB, Erman JE.The binding of horse heart cytochrome c to yeast cytochrome c peroxidase in which the heme group was replaced by protoporphyrin IX was determined by a fluorescence quenching technique. The association between ferricytochrome c and cytochrome c peroxidase was investigated at pH 6.0 in cacodylate/KNO3 buffers. Ionic strength was varied between 3.5 mM and 1.0 M. No binding occurs at 1.0 M ionic strength although there was a substantial decrease in fluorescence intensity due to the inner filter effect. After correcting for the inner filter effect, significant quenching of porphyrin cytochrome c pe...
Can the product of the theta gene be a real globin?
Nature    October 1, 1987   Volume 329, Issue 6138 465-466 doi: 10.1038/329465a0
Clegg JB.A new member (theta 1, or psi alpha) of the alpha-globin gene family has recently been identified in a number of species. In higher primates the theta 1 gene has all the structural features apparently necessary for expression, and it appears to have long been under strong selective constraints which suggests that it could still be, or recently have been, a functional gene. No corresponding 'globin' has yet been identified, however. In some other species, galago and rabbit for example, the theta 1 and psi alpha genes have accumulated enough inactivating mutations for them to be considered genui...
Ethoxyformylation of histidine residues in equine growth hormone.
International journal of peptide and protein research    September 1, 1987   Volume 30, Issue 3 365-370 doi: 10.1111/j.1399-3011.1987.tb03343.x
Fukushima JG, Cascone O, Santomé JA, Biscoglio de Jimenez Bonino MJ.Reactivity of histidine residues in equine growth hormone to ethoxyformic anhydride was studied. The existence of two kinetically different sets was demonstrated: one of them including only the slow reacting histidine 169 (k = 0.164 min-1) and the other containing fast reacting histidines 19 and 21 (k = 0.892 min-1). A correlation between the decrease in the capacity to compete with 125I-labeled hormone for rat liver binding sites and the degree of ethoxyformylation of the fast group was found. Circular dichroism studies indicated no significant conformational changes in the protein with all t...
Site-directed chemical modification of horse cytochrome c results in changes in antigenicity due to local and long-range conformational perturbations.
The Journal of biological chemistry    August 25, 1987   Volume 262, Issue 24 11591-11597 
Cooper HM, Jemmerson R, Hunt DF, Griffin PR, Yates JR, Shabanowitz J, Zhu NZ, Paterson Y.Comparative binding studies with peptide fragments of the whole antigen, or with evolutionarily related intact proteins with varying degrees of sequence homology, have been used extensively to map antigenic sites on proteins to the resolution of single amino acid residues. These methods are limited, however, since high affinity antibodies will often not react with peptides and evolutionarily related proteins are available for only a few antigens. In this study we use site-directed chemical modification of horse cytochrome c to identify residues involved in the binding sites of four monoclonal ...
Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c.
The Biochemical journal    August 15, 1987   Volume 246, Issue 1 43-54 doi: 10.1042/bj2460043
Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ.Magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K of horse heart cytochrome c are reported at a series of pH values between 7.8 and 11.0, encompassing the alkaline transition. The effect of glassing agents on the e.p.r. spectrum at various pH values is also reported. Comparison of these results with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin support the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c. The m.c.d. and e.p.r. spectra of horse heart cytochrome c ...
Multiple myeloma in a horse.
Journal of the American Veterinary Medical Association    August 1, 1987   Volume 191, Issue 3 337-339 
MacAllister C, Qualls C, Tyler R, Root CR.Multiple myeloma was diagnosed in a horse on the basis of clinical signs, protein electrophoresis pattern, Bence-Jones proteinuria, and radiographic changes in bone. The horse had mild depression, weight loss, edema of the distal portion of the left hind limb, anemia, hyperproteinemia, and monoclonal gammopathy in the beta 2 region. Radiographically, punctate cortical lysis of bone was seen. Specific treatment for the multiple myeloma was not attempted and the horse was euthanatized.
Structural and functional studies on ferritins.
Biochemical Society transactions    August 1, 1987   Volume 15, Issue 4 744-748 doi: 10.1042/bst0150744
Harrison PM, Ford GC, Rice DW, Smith JM, Treffry A, White JL.No abstract available
The role of aromatic side chain residues in micelle binding by pancreatic colipase. Fluorescence studies of the porcine and equine proteins.
The Biochemical journal    August 1, 1987   Volume 245, Issue 3 821-829 doi: 10.1042/bj2450821
McIntyre JC, Hundley P, Behnke WD.Fluorescence techniques have been employed to study the interaction of porcine and equine colipase with pure taurodeoxycholate and mixed micelles. Nitrotyrosine-55 of porcine colipase is obtained by modification with tetranitromethane (low excess, in the presence of taurodeoxycholate) of the protein followed by gel filtration and ion-exchange chromatography. Verification of the residue modified was obtained by h.p.l.c. peptide purification and sequence analysis. Reduction and quantitative reaction with dansyl chloride yields a fluorescent derivative that is twice as active in conjunction with ...
The binding domain on horse cytochrome c and Rhodobacter sphaeroides cytochrome c2 for the Rhodobacter sphaeroides cytochrome bc1 complex.
Biochemistry    July 14, 1987   Volume 26, Issue 14 4501-4504 doi: 10.1021/bi00388a049
Hall J, Zha XH, Yu L, Yu CA, Millett F.The interaction of the Rhodobacter sphaeroides cytochrome bc1 complex with Rb. sphaeroides cytochrome c2 and horse cytochrome c was studied by using specific lysine modification and ionic strength dependence methods. The rate of the reactions with both cytochrome c and cytochrome c2 decreased rapidly with increasing ionic strength above 0.2 M NaCl. The ionic strength dependence suggested that electrostatic interactions were equally important to the reactions of the two cytochromes, even though they have opposite net charges at pH 7.0. In order to define the interaction domain on horse cytochro...
Calcium balance and dietary protein content.
Equine veterinary journal    July 1, 1987   Volume 19, Issue 4 265 doi: 10.1111/j.2042-3306.1987.tb01400.x
Frape DL.No abstract available
The amino acid sequence of an amyloid fibril protein AA isolated from the horse.
Scandinavian journal of immunology    July 1, 1987   Volume 26, Issue 1 79-84 doi: 10.1111/j.1365-3083.1987.tb02237.x
Sletten K, Husebekk A, Husby G.The amino acid sequence of the amyloid fibril protein AA from horse was established from characterization of cyanogen bromide fragments, tryptic peptides, and a peptide derived from a digest with Staphylococcus aureus V8 proteinase. The protein was found to consist of 80 amino acid residues. Sequence homologies with protein AA from other species were very striking, and revealed an insertion of two amino acid residues between positions 72 and 73. In position 44, two amino acid residues were found which provide further evidence for a polymorphism in the amyloid fibril protein AA.
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