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 amino-acid sequence of beta-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): beta-lactoglobulins are retinol-binding proteins.
Biological chemistry Hoppe-Seyler    June 1, 1985   Volume 366, Issue 6 601-608 doi: 10.1515/bchm3.1985.366.1.601
Godovac-Zimmermann J, Conti A, Liberatori J, Braunitzer G.beta-Lactoglobulin isolated from horse colostrum is heterogeneous and contains two components: beta-lactoglobulin I and beta-lactoglobulin II. These two proteins are monomeric and show differences in their electrophoretic mobilities, chain lengths and primary structures. The complete amino-acid sequence of beta-lactoglobulin II was determined by automated Edman degradation of the intact protein and of the peptides derived from these by digestion with trypsin or chymotrypsin and by chemical cleavage with cyanogen bromide. Unlike other beta-lactoglobulins which contain 162 amino acids, horse bet...
Changes in the synovia after the intra-articular injection of sodium hyaluronate into normal horse joints and after arthrotomy and experimental cartilage damage.
Australian veterinary journal    June 1, 1985   Volume 62, Issue 6 182-184 doi: 10.1111/j.1751-0813.1985.tb07290.x
Hilbert BJ, Rowley G, Antonas KN, McGill CA, Reynoldson JA, Hawkins CD.Sodium hyaluronate was injected into normal horse joints and joints that had undergone an arthrotomy and experimental cartilage damage. The elimination half-life for hyaluronic acid in normal joints was found to be approximately 96 h. The injection caused a non-significant increase (42%) in synovial fluid protein concentration and a fall in the intrinsic viscosity of the fluid. In the arthrotomy group the synovial fluid hyaluronic acid concentration fell after surgery but it was unaffected by the injection of sodium hyaluronate. An initial rise in the intrinsic viscosity of the synovial fluid ...
The sequence of equine muscle carbonic anhydrase.
The Journal of biological chemistry    May 25, 1985   Volume 260, Issue 10 6129-6132 
Wendorff KM, Nishita T, Jabusch JR, Deutsch HF.The sequence of equine muscle carbonic anhydrase (CA-III) has been determined. The 2 reactive cysteines of the 5 such residues have been localized. A strong sequence homology to other mammalian carbonic anhydrases exists, and 91% of the residues in the equine and bovine muscle forms are identical.
[Isolation and properties of a nonspecific adhesive factor from the blood serum of warm-blooded animals and man].
Zhurnal obshchei biologii    May 1, 1985   Volume 46, Issue 3 389-400 
Reznikova MM, Iamskova VP.No abstract available
Microtubular mass defect of spermatozoa in the stallion.
American journal of veterinary research    May 1, 1985   Volume 46, Issue 5 1121-1125 
Heath E, Aire T, Fujiwara K.A microtubular mass (MM) defect was found in the spermatozoa of 7 Standardbred stallions; 3 stallions were sons of the same sire. Two of these 3 stallions and 2 other stallions (for a total of 4 out of the 7 stallions) were considered subfertile when the defect was first observed. Fertility improved with time, either during the first breeding season or when a given stallion was used less frequently; however, the MM defect persisted, consisting of tortuous arrays of small abnormal microtubules visible only by transmission electron microscopy. The MM probably contained the protein tubulin as ind...
Immunologically reactive proteins of Streptococcus equi.
Infection and immunity    April 1, 1985   Volume 48, Issue 1 29-34 doi: 10.1128/iai.48.1.29-34.1985
Timoney JF, Trachman J.Immunologically reactive proteins in acid extracts and culture supernatants of Streptococcus equi were recognized through a combination of chromatographic and immunologic procedures. Both high- and low-molecular-weight components of each of these protein preparations were protective for mice and were, therefore, presumed to contain a variety of hydrolytic products or fragments of the M protein of S. equi. Convalescent horse sera that exhibited strong bactericidal activity for S. equi always reacted with polypeptides in the molecular weight range of 24,000 to 29,000, whereas preinfection sera d...
Changes in blood constituents accompanying exercise in polo horses.
The Cornell veterinarian    April 1, 1985   Volume 75, Issue 2 297-302 
Craig L, Hintz HF, Soderholm LV, Shaw KL, Schryver HF.There have been several studies of biochemical changes in horses doing intense exercise such as Thoroughbred and Standardbred racehorses and in horses performing exercise over a long period of time such as endurance horses and three-day eventing horses, but we are not aware of studies with polo horses. Blood samples were taken from 18 polo horses at rest, immediately after playing 2 chukkers of indoor polo, and after a 15 minute rest period. Each horse was studied at 2 different games. The blood samples were analyzed for lactic acid, protein, sodium, potassium, chloride, calcium, phosphorus, H...
Antigenic determinants of acylphosphatase from porcine skeletal muscle.
Journal of biochemistry    April 1, 1985   Volume 97, Issue 4 1143-1154 doi: 10.1093/oxfordjournals.jbchem.a135159
Kizaki T, Mizuno Y, Takasawa T, Shiokawa H.Analysis of the quantitative precipitin reaction of acylphosphatase from porcine skeletal muscle with rabbit antiserum indicated the presence of at least two antigenic determinants on the porcine enzyme molecule. Immunological cross-reactivities of acylphosphatases from equine and rabbit skeletal muscles were examined. In double immunodiffusion with the antiserum, the precipitin lines of the porcine and equine enzymes completely fused, while the rabbit enzyme gave no precipitin line. The reaction between the 125I-labeled porcine enzyme and its antibody was inhibited to the same extent by the p...
Hybrids from equine LH: alpha enhances, beta diminishes activity.
Molecular and cellular endocrinology    April 1, 1985   Volume 40, Issue 1 69-77 doi: 10.1016/0303-7207(85)90159-5
Bousfield GR, Liu WK, Ward DN.LH hybrids were prepared by combining eLH alpha and eLH beta with the corresponding subunits of oLH, pLH and hCG. Recombinants were isolated by gel filtration and assessed by SDS-polyacrylamide gel electrophoresis under both dissociating and non-dissociating conditions. All combinations of subunits produced hybrid LH molecules. Hybrids prepared by combining eLH beta with oLH alpha, pLH alpha or hCG alpha were very inactive in rat radioligand and Leydig cell in vitro bioassays. Hybrids prepared with eLH alpha were very active in both assays. The greatest potentiating activity was observed when ...
Iron deposition in apoferritin. Evidence for the formation of a mixed valence binuclear iron complex.
The Journal of biological chemistry    March 10, 1985   Volume 260, Issue 5 2926-2929 
Chasteen ND, Antanaitis BC, Aisen P.A preliminary EPR investigation of iron accumulation in apoferritin has identified paramagnetic species generated during the early stage of iron deposition within the apoprotein shell. A featureless resonance at g' = 4.3, attributable to solitary high spin Fe3+ ions bound to the protein, is generated when Fe(II) is added to apoferritin at a level of 0.5 Fe/subunit (12 Fe/molecule) followed by air oxidation. This resonance accounts for 36% of the added iron. The remainder is EPR-silent and is probably present as oligomeric Fe3+ species. The intensity of the g' = 4.3 signal is reduced 3-fold upo...
Laboratory evaluation of aqueous humor in the healthy dog, cat, horse, and cow.
American journal of veterinary research    March 1, 1985   Volume 46, Issue 3 657-659 
Hazel SJ, Thrall MA, Severin GA, Lauerman LH, Lavach JD.Using routinely available clinical laboratory methods, aqueous humor samples were evaluated from 12 healthy dogs, 15 healthy cats, 7 healthy horses, and 6 healthy cows. Aqueous humor was almost acellular; cells that were present had degenerated beyond recognition. Protein concentration was low; only albumin was detectable on electrophoresis. Creatine phosphokinase and lactate dehydrogenase isoenzymes were not detected. Artifacts induced by sampling were insignificant compared with alterations in aqueous humor composition that occur with ocular diseases.
[Comparative characteristics of the vitreous body proteins in vertebrates].
Zhurnal evoliutsionnoi biokhimii i fiziologii    March 1, 1985   Volume 21, Issue 2 130-133 
Zorin NA, Rykov VA, Potekhin VK, Savinykh VI, Chirikova TS.Using disc-electrophoresis in polyacrylamide gel and immunochemical methods, studies have been made on proteins from the vitreous body of mammals (albino mouse, rat, guinea pig, pig, dog, cat), birds (hen), amphibians (the frog Rana ridibunda) and fish (the perch Perca fluviatilis). It was found that vitreous body proteins in man and animals include both the specific proteins and those of the blood serum. During evolution, specific antigens of the vitreous body attained strict species specificity, although some of them preserved the initial properties.
Mucosal nasopharyngeal immune responses of horses to protein antigens of Streptococcus equi.
Infection and immunity    March 1, 1985   Volume 47, Issue 3 623-628 doi: 10.1128/iai.47.3.623-628.1985
Galan JE, Timoney JF.Mucosal nasopharyngeal immunoglobulin A (IgA) and IgG responses to proteins of Streptococcus equi were studied in horses after the experimental production of strangles. S. equi-specific IgA and IgG titers in nasopharyngeal mucus were much higher in samples from animals 1 to 2 weeks after challenge than in samples from control animals. Although IgA was the major immunoglobulin in nasal mucus, there was more antibody activity associated with IgG as measured by radioimmunoassay. Great differences between the specificities of antibodies in nasal mucus and in serum were detected. IgA and IgG of muc...
Inhibition of lipases by proteins. A kinetic study with dicaprin monolayers.
The Journal of biological chemistry    February 25, 1985   Volume 260, Issue 4 2268-2273 
Gargouri Y, Pieroni G, Rivière C, Sugihara A, Sarda L, Verger R.We report further investigations on protein inhibition of pancreatic and microbial lipases carried out with the monolayer technique. When beta-lactoglobulin A, melittin, serum albumin, myoglobin, and a protein inhibiting lipase from soybean were preincubated with a dicaprin film at a surface pressure of 35 dynes/cm, no activity was detected with horse pancreatic or Rhizopus delemar lipases. By contrast, Rhizopus arrhizus and Geotrichum candidum lipase activities were not impaired under the same conditions. Experiments using mixed lipid-protein film transfer clearly show that the inhibition of ...
Pharmacokinetics and bioavailability of cefazolin in horses.
American journal of veterinary research    February 1, 1985   Volume 46, Issue 2 348-352 
Sams RA, Ruoff WW.The pharmacokinetics and bioavailability of cefazolin given (IV, IM) to horses at the dosage of 11 mg/kg were investigated. The disposition of cefazolin given by IV route was characterized by a rapid disposition phase with a half-life of 5 to 10 minutes and a subsequent slower elimination phase with a half-life of 35 to 46 minutes. The total plasma clearance of cefazolin averaged 5.51 ml/min/kg and was due mainly to renal clearance (5.39 ml/min/kg) of unchanged drug. The volume of distribution at steady-state averaged 188 ml/kg. Plasma protein binding of cefazolin at a concentration of 10 micr...
Native and carboxymethylated horse liver alcohol dehydrogenase: electrostatic fields and the Pauling strain-distortion hypothesis.
Progress in clinical and biological research    January 1, 1985   Volume 174 169-179 
Dunn MF, Dahl KH.No abstract available
The amino acid sequence of equine milk lysozyme.
Biochemistry international    January 1, 1985   Volume 10, Issue 1 23-31 
McKenzie HA, Shaw DC.The amino acid sequence of equine milk lysozyme has been elucidated. The study involves the determination of the sequence of the N-terminal region of the whole protein, cyanogen bromide fragments, tryptic and chymotryptic peptides and fragments produced by chemical cleavage after tryptophan residues. The protein consists of a single chain of 129 amino acid residues and has a Mr of 14647. While equine milk lysozyme has the essential features of a c(chick)-type lysozyme, there is only 51% sequence homology with human milk lysozyme and 50% with domestic hen egg white lysozyme. Some of the implica...
Influence of several perturbants on the rate of autoxidation of horse heart ferrocytochrome c.
The International journal of biochemistry    January 1, 1985   Volume 17, Issue 1 119-122 doi: 10.1016/0020-711x(85)90095-3
Harrington JP, Carrier TL.The effect of several different types of perturbants and pH on the rate of autoxidation of horse heart ferrocytochrome c was investigated. The kinetic behavior is unique to each perturbant used. Rates of autoxidation followed first-order kinetics over the time span (0-180 min) studied. The Cl- and Br- anions exhibit an initial increase in the rate of autoxidation up to 100 mM, followed by a decrease in kinetics at 500 mM anion concentration. The ClO4- anion exhibits only an increase in the rate of autoxidation with increasing ionic strength, where as, propylurea, a hydrophobic perturbant, is n...
Alkylation of bronchiolar epithelial cells by 3-methylindole metabolites in the horse.
Toxicology letters    January 1, 1985   Volume 24, Issue 1 25-32 doi: 10.1016/0378-4274(85)90135-3
Becker GM, Nocerini MR, Carlson JR, Breeze RG.Autoradiographs of horse-lung explants incubated with [3H]3-methylindole (3MI) showed 8 times greater labeling per area to bronchiolar epithelial cells than to the interalveolar septa. Incubations of horse-lung microsomes with [14C]3MI resulted in alkylation of microsomal proteins, which could be reduced by exogenous glutathione. An apparent covalent adduct of glutathione and 3MI was isolated from these incubations. These results suggest that the target cells of 3MI-induced injury in the horse, the bronchiolar epithelial cells, are alkylated by an electrophilic 3MI intermediate.
Characteristics of Mycoplasma strains isolated from stallion semen.
Archivum immunologiae et therapiae experimentalis    January 1, 1985   Volume 33, Issue 6 851-856 
Zgórniak-Nowosielska I, Kosiniak K, Slagowska A.Eleven mycoplasma strains were isolated from the semen of 24 stallions. Eight of these strains were identified as Mycoplasma equigenitalium. Three strains which hydrolized arginine could not be identified. The growth inhibition test with immune sera against M. arginini and M. equirhinis was negative. Antibiotic sensitivity test showed that all strains were sensitive to four antibiotic of tetracycline group (oxytetracyclin, minocycline, transcycline and vibramycin). Lincomycin and gentamycin appeared to be the most active against all the strains. Comparative analysis of routine semen examinatio...
Seasonal changes in blood serum protein fractions and in activity of AspAT and AlAT in Arabian brood mares and their foals.
Comparative biochemistry and physiology. A, Comparative physiology    January 1, 1985   Volume 82, Issue 1 167-178 doi: 10.1016/0300-9629(85)90722-4
Gill J, Jakubów K, Kompanowska-Jezierska E, Kott A, Szumska D.In 34 pure breed Arabian horses divided into four groups (Gr. I--10 pregnant mares, Gr. II--7 barren mares, Gr. III--10 foals born in 1981, Gr. IV--7 foals born in 1982) seasonal changes in total blood serum protein, its electrophoretic fractions and the activity of AspAT and AlAT were studied. Seasonal cyclicity was found in all groups in the amount of total serum proteins, and alpha 2- and beta 1-globulin fractions. Cyclicity was found in the level of albumin and activity of AspAT in three groups, not Gr. II, and in gamma-globulin, not Gr. IV. beta 2-globulin and AlAT cyclicity was found in ...
Horse leucocyte proteinase-inhibitor system. Kinetic parameters of the inhibition reaction.
The International journal of biochemistry    January 1, 1985   Volume 17, Issue 4 509-513 doi: 10.1016/0020-711x(85)90147-8
Dubin A, Potempa J, Silberring J.Horse leucocyte neutral proteinase inhibitor reacts with all tested elastases at the molar ratios of 1:1 and yielding stable complexes (Ki = 10(-10) M). The above reactions are very rapid, characterized by the high values of association rate constant kon = 10(7) M-1s-1.
Unfolding-refolding transition of a hinge bending enzyme: horse muscle phosphoglycerate kinase induced by guanidine hydrochloride.
Biochemistry    December 18, 1984   Volume 23, Issue 26 6654-6661 doi: 10.1021/bi00321a057
Betton JM, Desmadril M, Mitraki A, Yon JM.The unfolding-refolding transition of horse muscle phosphoglycerate kinase induced by guanidine hydrochloride was studied under equilibrium conditions using four different signals: fluorescence intensity at 336 nm, UV difference absorbance at 286 and 292 nm, ellipticity at 220 nm, and enzyme activity. From the following arguments, we found that the process deviates from a two-state model and intermediates are significantly populated even at equilibrium: (1) the noncoincidence of the transition curves and (2) the asymmetry of the transition curve obtained from CD measurements. From these differ...
The primary structure of monomeric beta-lactoglobulin I from horse colostrum (Equus caballus, Perissodactyla).
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    December 1, 1984   Volume 365, Issue 12 1393-1401 doi: 10.1515/bchm2.1984.365.2.1393
Conti A, Godovac-Zimmermann J, Liberatori J, Braunitzer G.beta-Lactoglobulin-like proteins were detected in horse colostrum and normal milk using immunological techniques. In contrast to the beta-lactoglobulins sequenced so far these proteins are monomeric and genetically not homogenous. In this paper we report the first primary structure of a monomeric beta-lactoglobulin from horse colostrum. By means of an automatic liquid-phase sequenator the sequence of peptides obtained by tryptic digestion and by cyanogen bromide cleavage was determined. A limited tryptic digestion and hydrolysis with chymotrypsin provided the necessary overlapping peptides. Th...
Cadmium/zinc relationships in kidney cortex and metallothionein of horse and red deer: histopathological observations on horse kidneys.
Environmental research    December 1, 1984   Volume 35, Issue 2 466-481 doi: 10.1016/0013-9351(84)90153-1
Holterman WF, de Voogt P, Peereboom-Stegeman JH.Cadmium and zinc were determined in kidney cortex of 63 horses and 51 red deer (Cervus elaphus). Cadmium and zinc were also determined in protein fractions obtained by Sephadex chromatography of kidney cortex from 10 horses and 4 red deer. Histopathological parameters in kidney cortex of horses were compared to cadmium content. The metal contents (on wet weight basis) in kidney cortex of the horses were 0.31 +/- 0.22 mmole Cd/kg (range 0.03-1.21) and 0.63 +/- 0.17 mmole Zn/kg (range 0.36-1.23). The Zn content increased with the Cd content, the Zn increase being less at higher concentrations. N...
The amino acid sequence of equine alpha-lactalbumin.
Biochemistry international    November 1, 1984   Volume 9, Issue 5 539-546 
Kaminogawa S, McKenzie HA, Shaw DC.The amino acid sequence of equine alpha-lactalbumin has been determined with the aid of an automatic sequencer. The protein chain consists of 123 amino acids and has a Mr of 14218. Elucidation of the structure involved sequence determination of native protein (residues 1-32), cyanogen bromide fragments, and tryptic, chymotryptic and S. aureus V8 proteolytic peptides. Approximately 67% of the residues are identical with corresponding residues of bovine alpha-lactalbumin B, and there is close homology with alpha-lactalbumin of other species.
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...
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