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.
Streptokinase-dependent delayed activation of horse plasminogen.
Biochimica et biophysica acta    December 6, 1982   Volume 709, Issue 1 19-27 doi: 10.1016/0167-4838(82)90416-2
Marcum JA, Highsmith RF, Kline DL.Complete activation of purified horse plasminogen to plasmin was obtained with a 1:10 molar ratio of streptokinase to plasminogen after 5 min of incubation at 37 degrees C. At a 1:1 molar ratio, maximal activity did not appear until 15-30 min, while at a ratio of 6:1 complete activation was delayed for 120-180 min. Gel filtration studies of isotopically labeled streptokinase and horse plasminogen suggest that the delay was due to impaired formation of a streptokinase-plasminogen complex. The predominant streptokinase moiety within the streptokinase-plasmin complex which forms from the streptok...
Serum protein binding of furosemide in several species.
Journal of veterinary pharmacology and therapeutics    December 1, 1982   Volume 5, Issue 4 293-294 doi: 10.1111/j.1365-2885.1982.tb00446.x
Neff-Davis CA, Davis LE.No abstract available
Correlation of parvalbumin concentration with relaxation speed in mammalian muscles.
Proceedings of the National Academy of Sciences of the United States of America    December 1, 1982   Volume 79, Issue 23 7243-7247 doi: 10.1073/pnas.79.23.7243
Heizmann CW, Berchtold MW, Rowlerson AM.The physiological role of the Ca2+-binding protein parvalbumin in skeletal muscle has been investigated by measuring the parvalbumin content by HPLC in a variety of mammalian muscles, including man, and comparing the results with the respective muscle relaxation properties and fiber type compositions. The parvalbumin concentrations were highest in the skeletal muscles of the smallest animal investigated (mouse, gastrocnemius: 4.9 g/kg), which has the highest relaxation speed, and lowest in the larger animals (horse, deep gluteal muscle: less than or equal to 0.001 g/kg) and man (vastus, tricep...
Characterization of the major antigens of Haemophilus equigenitalis (contagious equine metritis organism).
The Journal of hygiene    December 1, 1982   Volume 89, Issue 3 529-538 doi: 10.1017/s0022172400071102
Corbel MJ, Brewer RA.Immunoelectrophoresis of ultrasonically disrupted Haemophilus equigenitalis (contagious equine metritis organism) cells against rabbit and equine antisera disclosed at least 11 precipitating antigens. Two of these, a polysaccharide and a lipopolysaccharide-protein complex, were of high molecular weight and located on the cell surface. The remaining antigens were intracellular and were small- to medium-sized proteins. The surface antigens were the most significant in relation to the serological response in infected horses. They also reacted with sera from apparently healthy cattle, but the reas...
Serum protein electrophoresis in horses and ponies.
Equine veterinary journal    October 1, 1982   Volume 14, Issue 4 322-324 doi: 10.1111/j.2042-3306.1982.tb02443.x
Matthews AG.A method of electrophoresis of horse serum on agarose gels (pH 8.6) is described, together with a system for interpreting changes in the electrophoretic zones based upon the relative distribution of the major serum proteins. Differences in the protein composition of the individual electrophoretic zones of horses and ponies were recorded, although this variation probably reflects differences in management and the presence of subclinical disease.
Enzyme activities and protein concentration in the intraocular fluids of ten mammals.
Acta ophthalmologica    October 1, 1982   Volume 60, Issue 5 729-741 doi: 10.1111/j.1755-3768.1982.tb06733.x
Wurster U, Riese K, Hoffmann K.An attempt was made to establish normal values for the total protein concentrations and the enzyme activities of LDH, MDH and PGI in the intraocular fluids of rats, guinea pigs, rabbits, cats, dogs, sheep, cattle, pigs, horses and humans. Remarkably little species differences were noted in 9 of the 10 mammals with vitreal enzyme activities falling into a narrow range between 8.4 U/l (PGI, horse) and 92.4 U/l (MDH, guinea pig). All species obeyed the sequence aqueous less than vitreous less than serum with exception of the rat, where vitreous activities surpassed serum at least two-fold. The ve...
A comparison of chemical and electrophoretic methods of serum protein determinations in clinically normal domestic animals of various ages.
The Cornell veterinarian    October 1, 1982   Volume 72, Issue 4 416-426 
Green SA, Jenkins SJ, Clark PA.The biuret total protein method and a bromcresol green (BCG) albumin method were used on the Abbott ABA-100 chemistry analyzer to assay serum proteins in clinically normal cattle, sheep, ponies, pigs, and ducks. Total proteins were also read on a refractometer and mylar supported cellulose acetate electrophoresis was performed. Globulins and A/G ratios were calculated from the chemical method and the results compared with the electrophoretic method. Total protein, albumin and A/G ratios in the ponies, sheep and older cattle were in agreement between the two methods. The younger cattle and all ...
[Some physicochemical properties of native and polymerized glutaraldehyde-treated horse heart cytochrome c].
Ukrainskii biokhimicheskii zhurnal (1978)    September 1, 1982   Volume 54, Issue 5 497-501 
Skok MV, Denisiuk PV, Komissarenko SV.Glutaraldehyde treatment does not change the absorption of cytochrome c either in the visible or in UV spectra. It brings about the formation of dimers, trimers and high-polymeric forms of cytochrome c and shifts the pI of all cytochrome c isoelectric fractions to more acid pH. Polymerization also results in changes of kinetic parameters of cytochrome c benzidine reaction increasing its affinity to 3,3-diaminobenzidine with a simultaneous decrease in the effectiveness of H2O2 binding. These biochemical changes can be related to immunochemical differences of native and glutaraldehyde-treated cy...
Purification and identification of horse serum IgA.
Nihon juigaku zasshi. The Japanese journal of veterinary science    August 1, 1982   Volume 44, Issue 4 661-668 doi: 10.1292/jvms1939.44.661
Kurimoto T, Ikeda A, Tanaka K.ウマ分泌型IgA (初乳, 涙) の分離精製については, すでに報告されているが, ウマ血清IgAの分離精製に関する明確な手法を示した報告は見あたらない. われわれは, ウマ血清を脱塩, 硫安塩析し, ついでDEAEセルロース, 免疫吸着体のカラム操作により, 抗原性および分子サイズにおいて, IgG, IgG(T), IgM とは明らかに区別される免疫グロブリンを分離精製した. この免疫グロブリンは抗イヌIgAとの交差反応性により, IgAと同定された. さらに作製した抗分泌型...
Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin.
Biochemical and biophysical research communications    July 30, 1982   Volume 107, Issue 2 435-441 doi: 10.1016/0006-291x(82)91510-8
Dianoux AC, Freyssinet JM.No abstract available
An electrophoretic investigation of mammalian spermatid-specific nuclear proteins.
Journal of reproduction and fertility    May 1, 1982   Volume 65, Issue 1 163-170 doi: 10.1530/jrf.0.0650163
Lanneau M, Loir M.Using standardized methods for protein extraction and analysis, the testes of rams, bulls, goats, boars, stallions, rats, cats, hedgehogs, European mink and ferrets were examined for basic spermatid nucleoproteins by electrophoresis. The results suggest that differences exist in the total number of these proteins as well as in the number and amount of the cross-linked cystein-containing proteins. These differences appear to be more family-specific than species-specific.
A comparison of the serum protein electrophoretic patterns of young and adult animals.
Veterinary research communications    May 1, 1982   Volume 5, Issue 3 271-276 doi: 10.1007/BF02214993
Keay G, Doxey DL.Samples of serum from both young and adult normal cattle, sheep and horses were subjected to protein electrophoresis on agarose gel films. After processing, the stained electrophoretic patterns and densitometric traces of each species exhibited certain specific characteristics. The separations also revealed differences between young and adult animals of the same species. These age-related differences are described here.
Resonance-enhanced Raman identification of a ternary chemical intermediate during the equine liver alcohol dehydrogenase reduction of p-(dimethylamino)benzaldehyde.
Biochemistry    April 27, 1982   Volume 21, Issue 9 2193-2202 doi: 10.1021/bi00538a031
Jagodzinski PW, Funk GF, Peticolas WL.The nature of the binding of aromatic aldehyde and aromatic alcohol substrates to the catalytic zinc of equine liver alcohol dehydrogenase has been studied by using resonance-enhanced Raman spectroscopy. When an excess of both enzyme and coenzyme to substrate is used, a stable ternary chemical intermediate is formed between liver alcohol dehydrogenase and the reduced coenzyme, nicotinamide adenine dinucleotide, and the aldehyde, p-(dimethylamino)benzaldehyde, in the pH range 8.5-0.6. Resonance-enhanced Raman spectra clearly show that this same intermediate is formed between the excess enzyme, ...
The conformational transition of horse heart porphyrin c.
The Journal of biological chemistry    April 10, 1982   Volume 257, Issue 7 3864-3868 
Brems DN, Liu YC, Stellwagen E.The heme iron of horse heart cytochrome c was selectively removed using anhydrous HF. The product, porphyrin c, exhibits the viscosity, far ultraviolet circular dichroic, and fluorescence properties characteristic for native cytochrome c. However, porphyrin c is more susceptible to denaturation by guanidine hydrochloride and by heat than is the parent cytochrome. All of the conformational parameters of porphyrin c exhibit a common reversible transition centered at 0.95 m guanidine hydrochloride at 23 degrees C and pH 7.0. Guanidine denatured porphyrin c refolds in two kinetic phases having tim...
Pancreatic colipase: crystallographic and biochemical aspects.
European journal of biochemistry    April 1, 1982   Volume 123, Issue 2 347-354 doi: 10.1111/j.1432-1033.1982.tb19774.x
Pierrot M, Astier JP, Astier M, Charles M, Drenth J.A detailed study of the crystallization of hog and horse colipases has been undertaken. Several crystallographic varieties have been obtained and a 0.3-nm resolution structure determination is actually in progress. The sequence of the A form of horse colipase (one methionine) is given. From spectrophotometric experiments and sequence comparisons, the involvement of the aromatic residue in position 52 in the micelle binding site has been demonstrated.
Synthesis and properties of equine beta-melanotropin and its naturally occurring des-Asp analog.
International journal of peptide and protein research    April 1, 1982   Volume 19, Issue 4 327-333 doi: 10.1111/j.1399-3011.1982.tb02611.x
Izdebski J, Yamashiro D, Ng TB, Li CH.No abstract available
Protein utilisation in response to caecal corn starch in ponies.
Equine veterinary journal    April 1, 1982   Volume 14, Issue 2 149-152 doi: 10.1111/j.2042-3306.1982.tb02372.x
Reitnour CM.The influence of administering caecal corn starch (0.0, 0.2, 0.4 or 0.6 g/kg body weight/day) on protein utilisation in 4 ponies was analysed with a latin square experimental design. The basal diet was dehydrated alfalfa pellets. Determinations were made of nitrogen retention, protein and dry matter digestions, total plasma protein, plasma urea nitrogen, plasma ammonia and plasma-free amino acids. Twice daily administration of corn starch into the caecum resulted in an increased nitrogen retention (P less than 0.01). Maximum nitrogen retention was observed with the caecal administration of 0.4...
Effect of intra-articular injection of orgotein and saline solution on equine synovia.
American journal of veterinary research    April 1, 1982   Volume 43, Issue 4 594-597 
Wagner AE, McIlwraith CW, Martin GS.Orgotein was injected into the right intercarpal joint of each of 8 horses; the corresponding left joint was left alone (not injected) or was given an injection of normal saline solution. Injection with orgotein caused a transient, marked inflammatory response, evidenced by clinical signs and by increased leukocytes and total protein in the synovia (synovial fluid). Leukocyte numbers and total protein concentration were increased (P less than 0.010) in the orgotein-injected joints within 24 hours. However, saline solution alone also elicited a marked inflammatory response, manifested by increa...
Isolation and characterization of beta- and gamma-caseins from horse milk.
The Biochemical journal    April 1, 1982   Volume 203, Issue 1 131-139 doi: 10.1042/bj2030131
Visser S, Jenness R, Mullin RJ.Three groups of casein components were isolated from horse milk. Group I is almost insoluble at acid and neutral pH, and is rather heterogeneous on alkaline gels with or without sodium dodecyl sulphate. Group II shows strong similarity to beta-casein from other species, as concluded from its amino acid composition and its N- and C-terminal sequences. This group consists of five electrophoretically distinguishable forms, all containing ester phosphate groups but no carbohydrate. Group III is composed of C-terminal fragments of the beta-like (group II) fraction and probably arises from the actio...
Serum and intracellular retinol in the equine.
The British journal of nutrition    March 1, 1982   Volume 47, Issue 2 273-280 doi: 10.1079/bjn19820036
Sklan D, Donoghue S.1. Serum and intracellular distribution of retinol was determined in equines maintained on four levels of vitamin A intake. 2. The form of retinol transported in serum was determined by gel filtration and chromatography to be a complex of retinol bound to a protein of molecular weight (MW) of approximately 20000, which was in turn complexed probably with prealbumin to yield a complex with a MW of 75000 to 80000. 3. Increasing dietary vitamin A levels enhanced the concentration of lipoprotein-bound retinyl esters in the plasma. 4. Vitamin A in the liver cytosol was found predominantly as retiny...
Milk production of quarter horse mares during 150 days of lactation.
Journal of animal science    March 1, 1982   Volume 54, Issue 3 496-499 doi: 10.2527/jas1982.543496x
Gibbs PG, Potter GD, Blake RW, McMullan WC.Milk production was measured in fourteen Quarter Horse mares at seven stages of a 150-d lactation period. Mares were divided into two groups of seven and fed diets containing either soybean meal or soybean meal and urea as nitrogen supplements. Rations were isocaloric, contained approximately 12.5% crude protein and were fortified with vitamins and minerals. Daily milk yield was estimated by the weigh-suckle-weigh method and milk composition was determined from samples taken by hand milking. Average daily milk yield ranged from 11.8 kg in early lactation to 9.8 kg in late lactation. Difference...
Renal dysfunction in a case of purpura haemorrhagica.
The Veterinary record    February 27, 1982   Volume 110, Issue 9 211 doi: 10.1136/vr.110.9.211
A four-year-old thoroughbred was presented with clinical manifestations of purpura haemorrhagica. Evidence of renal involvement consistent with glomerulopathy and nephrotic syndrome, characterized by heavy proteinuria and azotaemia, became apparent and may have been exacerbated by diuretic therapy. Autopsy revealed membrano- and mesangial proliferative glomerulonephritis and chronic pleuritis. Circulating immune complexes may have been responsible for the renal diseases and the purpura.
Purification of horse eosinophil peroxidase.
Biochimica et biophysica acta    February 18, 1982   Volume 701, Issue 2 185-191 doi: 10.1016/0167-4838(82)90112-1
Jörg A, Pasquier JM, Klebanoff SJ.Eosinophil peroxidase (donor: hydrogen-peroxidase oxidoreductase, EC 1.11.1.7) was isolated in a highly purified form (415/280 nm ratio, 1.05) from horse peripheral blood eosinophil. Eosinophil peroxidase was extracted from intact eosinophils (98-100% purity) or isolated eosinophil granules with 0.05 M acetate buffer (pH 4.7)/0.18 M NaCl and purified by chromatography on Sephadex G-200 and carboxymethylcellulose. Final elution was with 0.05 M acetate buffer (pH 4.7)/ 1 M NaCl. Horse eosinophil peroxidase is a strongly basic protein with bacterial properties when combined with H2O2 and iodide, ...
Renal dysfunction in a case of purpura haemorrhagica in a horse.
The Veterinary record    February 13, 1982   Volume 110, Issue 7 144-146 doi: 10.1136/vr.110.7.144
Roberts MC, Kelly WR.A four-year-old thoroughbred was presented with clinical manifestations of purpura haemorrhagica. Evidence of renal involvement consistent with glomerulopathy and nephrotic syndrome, characterised by heavy proteinuria and azotaemia, became apparent and may have been exacerbated by diuretic therapy. Autopsy revealed membrano- and mesangial proliferative glomerulonephritis and chronic pleuritis. Circulating immune complexes may have been responsible for the renal diseases and the purpura.
Analysis of equine thoracic fluid.
Veterinary clinical pathology    January 1, 1982   Volume 11, Issue 1 13-17 doi: 10.1111/j.1939-165x.1982.tb00813.x
Wagner AE, Bennett DG.Eighteen clinically normal horses were used to study the characteristics of normal thoracic fluid. Thoracic fluid was obtained from each horse and was found to be similar to equine abdominal fluid. Total leukocytes averaged 3994/ul, total protein 1.8 g/dl, and specific gravity 1.015. Analysis of thoracic fluid from 16 horses with clinical signs of thoracic disease showed abnormalities in every case. Thoracic fluid analysis alone determined a specific diagnosis in 50% of the cases.
Simultaneous isolation and partial characterization of antithrombin III and alpha 1-proteinase inhibitor from horse plasma.
Acta biochimica Polonica    January 1, 1982   Volume 29, Issue 1-2 95-103 
Kurdowska A, Koj A, Jaśkowska M.No abstract available
Serum proteins changes in horses infected with surra.
Revue d'elevage et de medecine veterinaire des pays tropicaux    January 1, 1982   Volume 35, Issue 2 147-151 
Raza MA, Rehman ZU, Chaudhry AH, Gilani AH, Nawaz M.No abstract available
Purification of horse muscle acylphosphatase antibodies by affinity chromatography.
Physiological chemistry and physics    January 1, 1982   Volume 14, Issue 3 307-311 
Berti A, Liguri G, Stefani M, Nassi P, Ramponi G.Horse muscle acylphosphatase antibodies were obtained by immunizing rabbits with the highly purified antigen cross-linked with glutaraldehyde. Specific antibodies were purified from the immunoglobulin fraction by affinity chromatography using a matrix coupled with the pure antigen as immunoadsorbent. The purified antibodies were partially characterized by immunodiffusion and immunoprecipitin techniques. These antibodies could be used to study aspects of the muscle acylphosphatase structure, localization and other biological properties.
[Purification of alpha-1,4 leads to 1,4-glucosyltransferase from horse blood serum].
Polskie archiwum weterynaryjne    January 1, 1982   Volume 23, Issue 3 65-72 
Kotoński B.The purification of alpha-1,4-1,4-glucosyltransferase from the equine serum is presented. Ion-exchange chromatography on DE-11, DE-32 and CM-32 celluloses was applied in the successive steps of isolation. Gel-filtration on Bio-Gel P-200 was the last step of purification; it gave the protein which was homogeneous on disc polyacrylamide gel electrophoresis. The purification degree was of the order 2100 at about 40% yield.
[Properties of alpha-1,4 leads to -glucosyltransferase from the muscles and blood serum of horses].
Polskie archiwum weterynaryjne    January 1, 1982   Volume 23, Issue 3 73-85 
Dzongowska-Dzongu T, Kotoński B, Hutny J.Alpha-1,4 leads to 1,4-glucosyltransferase preparations from horse muscles and serum were studied. The enzyme proteins from both tissues are very similar. Both proteins have a molecular weight of 240 000 and consist of four subunits of 60 000 daltons each. pH 5,0 is optimal for the activity. Only substrates with alpha-1, 4-linkages can serve as glucosyl donors for transferase reactions. Km values for both enzymes differ very slightly. At low substrate concentrations the hydrolytic activity can be found in addition to transferase reactions. At the concentration of the substrate higher than 40 m...
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