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.
Quantitation of the immunoglobulins in reproductive tract secretions of the mare.
Research in veterinary science    November 1, 1984   Volume 37, Issue 3 324-330 
Widders PR, Stokes CR, David JS, Bourne FJ.IgG, IgA, IgM and albumin concentrations were measured in serum, follicular fluid and oviductal, uterine and intestinal secretions of the horse. Follicular protein concentrations were found to be dependent on serum concentration and molecular size. Of the immunoglobulins only IgG was detectable in oviductal secretions, but IgG:albumin ratios did not differ significantly from those in serum. IgG, IgA and IgM were measured in uterine secretions, with IgG predominant. Serum transudation into uterine secretions was minimal. In intestinal secretions, IgA levels were slightly higher than IgG, with a...
Flunixin inhibits prostaglandin E2 production in equine inflammation.
Research in veterinary science    November 1, 1984   Volume 37, Issue 3 347-349 
Lees P, Higgins AJ.A model of acute inflammation was used in a cross-over study in Welsh mountain ponies to assess the actions of flunixin meglumine on selected components of a localised inflammatory reaction induced by injecting 0.5 ml of a 2 per cent carrageenin solution into subcutaneously implanted tissue cages. Samples of exudate were harvested at predetermined times between three and 48 hours. Increases in leucocyte numbers and protein concentration were not prevented by flunixin treatment. Prostaglandin E2-like activity was present in exudates from untreated ponies with the highest mean concentration occu...
Mare lactotransferrin: purification, analysis and N-terminal sequence determination.
FEBS letters    October 15, 1984   Volume 176, Issue 1 185-188 doi: 10.1016/0014-5793(84)80937-0
Jollès J, Donda A, Amiguet P, Jollès P.Mare lactotransferrin has been purified and analyzed. Its molecular mass is 81 kDa. A 28 amino acid long N-terminal sequence was established and a first series of comparisons with other transferrins was performed.
Effect of tyrosine modification on the biological and immunological properties of equine chorionic gonadotropin.
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)    October 1, 1984   Volume 177, Issue 1 42-46 doi: 10.3181/00379727-177-41909
Papkoff H, Murthy HM, Roser JF.The tyrosine residues of equine chorionic gonadotropin have been nitrated with tetranitromethane and the resulting effects on the biological and immunological activities of the hormone studied. All of the tyrosine residues in equine chorionic gonadotropin were found to react with tetranitromethane when a 100-fold molar excess of reagent was used or with an 8.6 molar excess in the presence of 5 M guanidine hydrochloride. Complete nitration abolished the biological activities and decreased the immunological activity of the hormone. The nitration of one tyrosine residue resulted in the loss of 70...
Isolation and partial characterization of bovine and equine factor D.
Molecular immunology    October 1, 1984   Volume 21, Issue 10 869-876 doi: 10.1016/0161-5890(84)90141-x
Blanchard DB, Leid RW.Bovine and equine factor D were purified to apparent homogeneity as evidenced by a single protein staining band on 7.5-17.5% SDS-PAGE slab gels under both reducing and non-reducing conditions. An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, ...
Antibacterial activity of mare uterine fluid.
Biology of reproduction    September 1, 1984   Volume 31, Issue 2 303-311 doi: 10.1095/biolreprod31.2.303
Strzemienski PJ, Do D, Kenney RM.Luminal fluid from the mare uterus was used to investigate its relation to antibacterial defenses. Uterine flushings were collected at Day 3 of estrus, Day 8 postovulation and Day 15 postovulation. Uterine proteins were concentrated by ultrafiltration, dialyzed and examined for chemotactic activity to neutrophils and for antibacterial properties. Serum taken at the time of flushing was dialyzed and studied in a similar manner. Neutrophil migration in response to serum from Day 3 estrus and Day 8 postovulation was increased (P less than 0.05) above controls. Uterine protein from Day 8 postovula...
Counterimmunoelectrophoresis for identification of equine urine.
American journal of veterinary research    September 1, 1984   Volume 45, Issue 9 1818-1821 
Edwards KE, Stevens S, Woodward CB, Tweeten KA.Counterimmunoelectrophoresis was evaluated as a method to distinguish urine of human origin from that of equine origin. The procedure used anti-equine serum and anti-human serum antibodies that had been solid-phase absorbed to eliminate species cross-reactivity. Counterimmunoelectrophoresis reliably detected contamination of equine urine by human urine to a level of 10% with a minimum sensitivity to about 2% contamination. Compared with double diffusion, counterimmunoelectrophoresis was approximately 10 to 15 times more sensitive in the detection of urine proteins.
Obtaining of pure transferrins D, M and R from equine serum and determination of transferrin level in relation to phenotype.
Acta physiologica Polonica    September 1, 1984   Volume 35, Issue 5-6 529-538 
Didkowski S, Kaminski M, Kerjan P, Tomaszewska-Guszkiewicz K, Zurkowski M.By the method of precipitation with Rivanol (2-ethoxy-6,9-diaminoacridine lactate) and ammonium sulphate followed by chromatography on DEAE cellulose three genetic variants of transferrin were purified from equine serum: D, M and R. Their molecular mass determined in this study was 80 000, and it was identical for all three variants, which differed slightly in their amino acid composition. The protein level was determined in the serum of 535 two-year-old thoroughbred English horses by the method of rocket immunoelectrophoresis using antibodies obtained against three transferrins. The individua...
Partial amino-acid sequence and cysteine reactivities of cytosolic aspartate aminotransferase from horse heart.
Biochimica et biophysica acta    August 28, 1984   Volume 789, Issue 1 51-56 doi: 10.1016/0167-4838(84)90059-1
Martini F, Angelaccio S, Barra D, Doonan S, Bossa F.Cytosolic aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from horse heart has five cysteine residues, two of which can be titrated with 5,5'-dithiobis(2-nitrobenzoid acid) in the native enzyme with no impairment of catalytic activity. The rate of modification is unaffected by the presence of substrates. Reaction with N-ethylmaleimide leads to loss of catalytic activity, the rate of inactivation being increased by the presence of substrates. Peptides containing 361 amino-acid residues (about 88% of the total number in the protein) have been isolated and ali...
Microheterogeneity of type II cAMP-dependent protein kinase in various mammalian species and tissues.
The Journal of biological chemistry    August 25, 1984   Volume 259, Issue 16 10596-10605 
Robinson-Steiner AM, Beebe SJ, Rannels SR, Corbin JD.Excluding autophosphorylated species, at least six forms of the regulatory subunit of type II cAMP-dependent protein kinase (RII) from various mammalian tissues were identified by sodium dodecyl sulfate (SDS) gel electrophoresis of purified samples and of crude preparations photoaffinity labeled with 8-azido[32P] cAMP and by gel filtration. After autophosphorylation some heart RII forms termed type IIA (bovine, porcine, equine, and dog) shifted to a more slowly migrating band on SDS gels while others termed type IIB (rat, guinea pig, rabbit, and monkey) did not detectably shift. Both subclasse...
Lysogeny and the immunologically reactive proteins of Streptococcus equi.
The Veterinary record    August 18, 1984   Volume 115, Issue 7 148-149 doi: 10.1136/vr.115.7.148
Timoney JF, Timoney PJ, Strickland KL.No abstract available
Antigenic reactivity of the major glycoprotein of equine infectious anemia virus, a retrovirus.
Virology    July 30, 1984   Volume 136, Issue 2 368-374 doi: 10.1016/0042-6822(84)90173-9
Montelaro RC, West M, Issel CJ.The immunogenic contributions of the carbohydrate and peptide portions of the major envelope glycoprotein of equine infections anemia virus, EIAV gp90, were analyzed by measuring the effects of specific glycosidase and protease digestions on the reactivity of the glycoprotein with immune sera from infected horses. The results of both direct and competitive radioimmunoassay demonstrated that immune sera contained antibodies reactive with both the carbohydrate and protein moieties of EIAV gp90, with the predominant reactivity apparently against the gp90 peptide epitopes. These results contrast w...
Ascorbate reduction of horse heart cytochrome c. A zero-energy reduction reaction.
The Journal of biological chemistry    July 10, 1984   Volume 259, Issue 13 8144-8150 
Myer YP, Kumar S.The ascorbate reduction of horse heart ferricytochrome c in 0.05 M phosphate + 0.25 M sodium sulfate, at pH 7.3, as a function of temperature, 12-36 degrees C, and at alkaline pH 8.4 using stopped flow technique has been examined. The data have been analyzed in terms of a two-step mechanism, binding followed by reduction (Myer, Y.P., Thallam, K.K., and Pande, A. (1980) J. Biol. Chem. 255, 9666-9673). At neutral pH and up to about 26 degrees C, the first order reduction constant is independent of temperature, i.e. with zero or near-zero activation energy. At higher temperatures, it becomes temp...
Analysis of the high- and low-spin Soret bands of horse-heart metmyoglobin complexes.
Biopolymers    July 1, 1984   Volume 23, Issue 7 1147-1167 doi: 10.1002/bip.360230702
Anusiem AC, Kelleher M.No abstract available
Mammary secretions in normal spontaneous and induced premature parturition in the mare.
Equine veterinary journal    July 1, 1984   Volume 16, Issue 4 256-259 doi: 10.1111/j.2042-3306.1984.tb01922.x
Leadon DP, Jeffcott LB, Rossdale PD.Total calcium, total protein, albumin and globulin content were determined in 49 samples of mammary secretions from 37 crossbred and Thoroughbred mares. The mares were divided into three categories: Group 1--post partum samples from spontaneous full term Thoroughbred deliveries (n = 20); Group 2--pre- and post partum samples from spontaneous full term Thoroughbred deliveries (n = 6); Group 3--pre- and post partum samples from induced premature deliveries in crossbred mares (n = 11). Calcium concentrations of the mammary secretions proved useful in predicting full term and also in assessment of...
The preparative separation of horse and human ferritins by chromatofocusing.
Journal of chromatography    June 1, 1984   Volume 292, Issue 2 454-457 doi: 10.1016/s0021-9673(01)83628-1
Addison JM, Lewis WG, Harrison PM.No abstract available
[Multiple forms of horse pepsin].
Biokhimiia (Moscow, Russia)    June 1, 1984   Volume 49, Issue 6 1026-1037 
Gonchar MV, Lavrenova GI, Rudenskaia GN, Gaĭda AV, Stepanov VM.Using ion-exchange and affinity chromatography and isoelectrofocusing, eight forms of pepsin with pI 1.6, 1.8, 2.1, 2.3, 2.6, 2.8, 3.2 and 3.6, were isolated from horse gastric juice. The molecular weights, amino acid composition, N-terminal sequence and functional activity of these multiple forms were determined. Partial primary structure of tryptic peptides of pepsin with pI 2.3 was investigated. The analyzed partial sequences of the forms with pI 1.8, 2.1, 2.3, and 2.6 have identical structures which differ from the amino acid sequence of pepsin with pI 3.2 by four substituents. In terms of...
Comparison of uterine protein content and distribution of bacteria in the reproductive tract of mares after intrauterine inoculation of Haemophilus equigenitalis or Pseudomonas aeruginosa.
American journal of veterinary research    June 1, 1984   Volume 45, Issue 6 1109-1113 
Strzemienski PJ, Benson CE, Acland HM, Kenney RM.Two groups of 3 mares were inoculated with Haemophilus equigenitalis or Pseudomonas aeruginosa on the 1st day of estrus. Uterine flushing samples were recovered on day 3 of estrus and day 8 after ovulation for each cycle. Mares were killed 22, 25, and 30 days after inoculation with P aeruginosa and 45, 46, and 49 days after inoculation with H equigenitalis. Pseudomonas aeruginosa was recovered from the uterus of 2 mares 48 hours after inoculation. Although the initial flushing sample of 1 of these 2 mares had an increased total protein concentration, there appeared to be little difference betw...
Kinetic study of CO and O2 binding to horse heart myoglobin reconstituted with synthetic hemes lacking methyl and vinyl side chains.
Archives of biochemistry and biophysics    June 1, 1984   Volume 231, Issue 2 366-371 doi: 10.1016/0003-9861(84)90399-0
Chang CK, Ward B, Ebina S.Carbon monoxide- and oxygen-binding rates and affinities were measured for horse heart myoglobins reconstituted with synthetic hemes lacking peripheral methyl and vinyl groups. There is an apparent correlation between heme size and ligand specificity, i.e. larger m values (ratios of CO vs O2 association rates, l'/k') with smaller hemes. However, this correlation broke down with the most dealkylated heme. This is interpreted as resulting from protein conformational changes altering the steric crowdedness at the O2-binding site. Spectral properties and autoxidation rates also corroborate this vi...
Chemotactic properties and protein of equine uterine fluid.
American journal of veterinary research    June 1, 1984   Volume 45, Issue 6 1205-1208 
Blue HB, Blue MG, Kenney RM, Merritt TL.Forty uterine fluid samples were obtained from 4 mares classified as resistant to uterine bacterial infection. The uterus of each mare was flushed with 50 ml of saline solution during estrus and diestrus of successive estrous cycles. Bacteria or fungi were isolated from 4 samples, and 7 additional samples were obtained from a mare with active intrauterine infection. Fluid volumes obtained during estrus (means = 40.3 +/- 11 ml) tended to be greater than those recovered during diestrus (means = 36.8 +/- 7.9 ml), but the difference was not significant. Concentrations and yields of protein in reco...
Relationship between paired plasma and serum viscosity and plasma proteins in the horse.
Research in veterinary science    May 1, 1984   Volume 36, Issue 3 360-363 
Allen BV, Blackmore DJ.The relationship between paired plasma and serum viscosity measurements and plasma proteins, including fibrinogen, were compared in 106 horses with both normal and abnormal serum protein levels. There is a highly significant positive correlation between serum viscosity and total serum proteins and total globulin levels. The difference between plasma and serum viscosity correlated well with clottable fibrinogen concentration. Albumin levels showed a negative correlation with plasma and serum viscosity, globulins and fibrinogen. Simultaneous estimation of serum and plasma viscosity improves the ...
Blood metabolite profiles of broodmares and foals.
Equine veterinary journal    May 1, 1984   Volume 16, Issue 3 192-196 doi: 10.1111/j.2042-3306.1984.tb01902.x
Rogers PA, Fahey GC, Albert WW.Serum amino acid profiles and other serum characteristics of broodmares and their foals wee studied. Compared with mares, foals had significantly higher concentrations of serum leucine, threonine, aspartic acid, asparagine, glutamic acid, glutamine, proline and tyrosine, glucose, cholesterol, creatinine and phosphorus. Foals had significantly less serum histidine, glycine, cystine, taurine, protein and urea nitrogen. Lysine and/or methionine supplementation of pregnant and lactating broodmare diets were conducted. Changes in serum amino acid profiles caused by dietary amino acid supplemented w...
Natural protease inhibitors: qualitative and quantitative assay by fibrinogen-agarose electrophoresis.
Analytical biochemistry    May 1, 1984   Volume 138, Issue 2 335-339 doi: 10.1016/0003-2697(84)90818-2
Pellegrini A, Hägeli G, Fretz D, von Fellenberg R.An electrophoretic procedure for the qualitative and quantitative assay of protein protease inhibitors is reported. This assay is particularly suited for investigations of crude biological materials when specific antisera are not available. The supporting medium consists of agarose into which denatured fibrinogen is incorporated as the substrate for proteases. The processing then is divided into two steps: (1) electrophoretic resolution of the inhibitor containing material and (2) detection of the inhibitor bands through their protease inhibiting activity. The inhibitor position is thus made v...
Equine cytomegalovirus: structural proteins of virions and nucleocapsids.
Virology    April 15, 1984   Volume 134, Issue 1 184-195 doi: 10.1016/0042-6822(84)90284-8
Caughman GB, Staczek J, O'Callaghan DJ.Enveloped virions and nucleocapsids of equine cytomegalovirus (ECMV; equine herpesvirus type 2) have been purified from the supernatants and the nuclear extracts of infected rabbit kidney (RK) cells, respectively, and their structural protein compositions have been analyzed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that ECMV nucleocapsids were composed of nine proteins (average molecular weights = 148K, 52K, 49.5K, 46K, 43.5K, 38.5K, 27K, 20K, and 18K), which together constituted 89% of the total nucleocapsid protein on the basis of incorporated 3H-labeled am...
Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
Biochemical genetics    April 1, 1984   Volume 22, Issue 3-4 357-367 doi: 10.1007/BF00484234
Jabusch JR, Deutsch HF.The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.
Alpha 2-macroglobulin from horse plasma. Purification, properties and interaction with certain serine proteinases.
Biochemistry international    April 1, 1984   Volume 8, Issue 4 589-596 
Dubin A, Potempa J, Silberring J.alpha 2-macroglobulin was isolated by polyethylene glycol precipitation, gel filtration on Sephacryl S-300 and DE-52 cellulose chromatography, with 20% yield. The preparation obtained was homogenous as tested by biochemical and immunological criteria. Its molecular mass was estimated at 800,000, comprising of four identical subunits. The isoelectric point of our preparation was 4.8 and two molecules of serine proteinases per 1 molecule of inhibitor were bound.
The isolation and characterization of a new elastase inhibitor, pre-alpha 2-elastase inhibitor, of the horse.
Biochimica et biophysica acta    March 1, 1984   Volume 797, Issue 3 336-342 doi: 10.1016/0304-4165(84)90254-x
Pellegrini A, Von Fellenberg R.A new and probably unique elastase inhibitor of horse serum was identified, purified to homogeneity and called pre-alpha 2-elastase inhibitor of the horse. Electrophoretically it migrated immediately in front of the alpha 2 position. Its molecular weight was 188 000 by pore limit polyacrylamide gel electrophoresis and 225 000 by Sephadex G-200 gel filtration. The inhibitor was composed of at least two non-identical polypeptide chains of Mr 68 400 and 87 600. A banding pattern of restricted heterogeneity focused between pH 4.9 and 5.2 was revealed by isoelectric focusing. Of 13 animal, microbia...
Arachidonic acid metabolites in carrageenin-induced equine inflammatory exudate.
Journal of veterinary pharmacology and therapeutics    March 1, 1984   Volume 7, Issue 1 65-72 doi: 10.1111/j.1365-2885.1984.tb00881.x
Higgins AJ, Lees P.The presence of cyclooxygenase products of arachidonic acid metabolism in carrageenin-induced inflammatory exudate was investigated in ponies using two models. In the first model, an inflammatory response was stimulated by injecting carrageenin into subcutaneously implanted polypropylene tissue cages and exudates were collected at five predetermined times between 3 and 48 h. In the second model, exudates were harvested at 6, 12 and 24 h from carrageenin-impregnated polyester sponges which had also been inserted beneath the skin. Prostaglandin (PG) E2, thromboxane (TX) B2 and the stable breakdo...
Characterisation of glycoproteins in the sweat of the horse (Equus caballus).
Research in veterinary science    March 1, 1984   Volume 36, Issue 2 231-234 
Eckersall PD, Beeley JG, Snow DH, Thomas A.The two major polypeptides H (Mr 49,000) and L (Mr 33,000) of equine sweat have been purified by gel filtration and characterised by gel electrophoresis and compositional analysis. Both H and L are glycoproteins containing sialic acid, neutral sugars, N-acetylglucosamine and N-acetylgalactosamine, but the two polypeptides differ considerably in the extent of glycosylation. H and L also differ in amino acid composition, but both contain only low levels of sulphur containing amino acids and histidine. These glycoproteins may behave as surfactants.
Purification of lutropin and follitropin in high yield from horse pituitary glands.
The Journal of biological chemistry    February 10, 1984   Volume 259, Issue 3 1911-1921 
Bousfield GR, Ward DN.A method has been developed for the purification of equine lutropin (eLH) and equine follitropin (eFSH) from horse pituitary glands which attains high yields of both hormones in contrast to previous methods that were devoted to one or the other with inferior recovery of the hormones. Two-pass chromatography over CM-Sephadex was used to separate eLH from eFSH. Subsequent steps employing QAE (quaternary amino-ethyl)-Sephadex chromatography and gel filtration on Sephacryl S-200 produced highly purified hormone preparations. Yields of purified eLH and eFSH were 110 and 60 mg/kg of frozen pituitari...
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