Analyze Diet

Topic:Amino Acids

Amino acids are organic compounds that serve as the building blocks of proteins and play crucial roles in various physiological processes in horses. They are essential for growth, tissue repair, and the synthesis of enzymes and hormones. Amino acids are categorized into essential amino acids, which must be obtained through the diet, and non-essential amino acids, which can be synthesized by the horse's body. Key essential amino acids for equine health include lysine, methionine, and threonine, which are vital for muscle development, immune function, and overall well-being. Amino acid levels can influence performance, recovery, and metabolic efficiency in horses, making their study important for optimizing equine nutrition and health management. This page compiles peer-reviewed research studies and scholarly articles that explore the role, metabolism, and clinical importance of amino acids in equine physiology and their impact on performance and health outcomes.
Characterization of a novel Na+-independent amino acid transporter in horse erythrocytes.
The Biochemical journal    April 1, 1985   Volume 227, Issue 1 13-20 doi: 10.1042/bj2270013
Fincham DA, Mason DK, Young JD.Horse erythrocytes are polymorphic with respect to L-alanine permeability. The present investigation compared the specificity, kinetics and cation-dependence of erythrocyte amino acid transport in two groups of thoroughbred horses, those with erythrocyte L-alanine permeabilities in the range 5-15 mumol/h per litre of cells (0.2 mM extracellular L-alanine, 37 degrees C) (transport-negative type) and those with L-alanine permeabilities in the range 450-700 mumol/h per litre of cells (transport-positive type). Transport-positive cells are shown to possess a novel high-affinity, stereospecific, Na...
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...
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...
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...
[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...
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...
Effects of dietary supplementation with butylated hydroxyanisole, cysteine, and vitamins B on tansy ragwort (Senecio jacobaea) toxicosis in ponies.
American journal of veterinary research    March 1, 1984   Volume 45, Issue 3 459-464 
Garrett BJ, Holtan DW, Cheeke PR, Schmitz JA, Rogers QR.Dried tansy ragwort, which contains pyrrolizidine alkaloids, was fed as 10% of a complete diet to ponies, with and without a mixture of additives. The additives provided a dietary supplement equivalent to 1% cysteine, 0.75% butylated hydroxyanisole, 200 micrograms of vitamin B12/kg of feed, and 5 mg of folic acid/kg of feed. The additives did not alter tansy ragwort toxicity, as assessed by survival time, liver changes, sulfobromophthalein (BSP) clearance rate, serum gamma-glutamyl transpeptidase activity, and plasma amino acid patterns. In ponies fed tansy ragwort, BSP clearance rate was a se...
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.
Difference in sizes of human compared to murine alpha-subunits of the glycoprotein hormones arises by four-codon gene deletion or insertion.
Endocrinology    February 1, 1983   Volume 112, Issue 2 482-485 doi: 10.1210/endo-112-2-482
Chin WW, Maizel JV, Habener JF.The sizes of the human and subhuman alpha-subunits of the glycoprotein hormones differ by four amino acids (hCG alpha, 92 amino acids; murine, equine, bovine, and ovine alpha, 96 amino acids). The shortening of the human alpha-subunit has been attributed to posttranslational proteolysis. We have recently determined the nucleotide sequences of the mRNAs encoding the precursors of the alpha-subunit of mouse TSH and rat gonadotropins using recombinant DNA techniques. In this report, we have compared these nucleotide sequences and their deduced amino acid sequences with those of the pre- alpha-sub...
Studies on prolactin 48: isolation and properties of the hormone from horse pituitary glands.
Archives of biochemistry and biophysics    January 1, 1983   Volume 220, Issue 1 208-213 doi: 10.1016/0003-9861(83)90402-2
Li CH, Chung D.Isolation of prolactin from equine pituitary glands has been described. It has a potency of 42 IU/mg in the pigeon crop-sac test and consists of 199 amino acids. The hormone has only four half-cystine residues in contrast to other mammalian prolactins which have six residues. From NH2-terminal sequence analysis and amino acid composition of cyanogen bromide fragments, the NH2-terminal disulfide loop is missing in the equine prolactin molecule. Circular dichroism spectra indicate that the alpha-helical content of equine prolactin appears to be lower (50%) than that found in the ovine hormone (6...
Structural and functional properties of the non-muscle tropomyosins.
Molecular and cellular biochemistry    January 1, 1983   Volume 57, Issue 2 127-146 doi: 10.1007/BF00849190
Côté GP.The non-muscle tropomyosins (TMs), isolated from such tissues as platelets, brain and thyroid, are structurally very similar to the muscle TMs, being composed of two highly alpha-helical subunits wound around each other to form a rod-like molecule. The non-muscle TMs are shorter than the muscle TMs; sequence analysis demonstrates that each subunit of equine platelet TM consists of 247 amino acids, 37 fewer than for skeletal muscle TM. The major differences in sequence between platelet and skeletal muscle TM are found near the amino and carboxyl terminal ends of the proteins. Probably as the re...
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, ...
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...
Systemic d-phenylalanine and d-leucine for effective treatment of pain in the horse.
The Canadian veterinary journal = La revue veterinaire canadienne    February 1, 1982   Volume 23, Issue 2 39-40 
McKibbin LS, Cheng RS.This study showed that subcutaneous injection of a solution of D-amino acids produced effective analgesia in horses. It is postulated that systemic D-phenylalanine and D-leucine may become one of the safe, effective and nonaddictive drugs for acute and chronic pain treatment. These D-amino acids cause analgesia by presumably preserving brain endorphins. They may bind reversibly to enkephalinases and prevent enzymatic degradation of enkephalins.
Lysine supplementation of diets for yearling horses.
Journal of animal science    December 1, 1981   Volume 53, Issue 6 1496-1503 doi: 10.2527/jas1982.5361496x
Ott EA, Asquith RL, Feaster JP.Forty-six Thoroughbred and Quarter Horse yearlings were used in two experiments designed to determine the amount of lysine in the concentrate necessary to promote maximum growth when fed the Coastal bermudagrass (Cynodon dactylon) hay provided at 1% body weight (BW)/day. In the first experiment, a 196-day trial, supplemental protein sources and analyses of the concentrates compared were: (1) soybean meal (SBM; 15.4% crude protein, .70% lysine); (2) SBM + .2% lysine (15.7% crude protein, .81% lysine), and (3) brewers dried grains + .2% lysine (15.9% crude protein, .59% lysine). Concentrate inta...
Crystallization and properties of creatine kinase from equine skeletal muscle.
Journal of biochemistry    May 1, 1981   Volume 89, Issue 5 1619-1631 doi: 10.1093/oxfordjournals.jbchem.a133357
Takasawa T, Fukushi K, Shiokawa H.A crystalline creatine kinase was obtained from equine skeletal muscle. The enzyme was homogeneous, as judged by ultracentrifugation and disc electrophoresis on polyacrylamide gel. The crystalline enzyme had a specific activity of 110 units per mg of protein, that is, 14-fold purification over the crude extract of equine skeletal muscle. The molecular weight of the enzyme was determined to be 84,600 by the conventional low-speed sedimentation equilibrium method, and s020,w was 5.32S. Eight cysteine residues were found on amino acid analysis, two of which were essential for the enzymatic activi...
Isolation and characterization of two glycophorins from horse erythrocyte membranes.
Journal of biochemistry    May 1, 1981   Volume 89, Issue 5 1593-1598 doi: 10.1093/oxfordjournals.jbchem.a133354
Murayama JI, Takeshita K, Tomita M, Hamada A.Crude glycophorin fraction was prepared from horse erythrocyte membranes by extraction with lithium diiodosalicylate and partition in aqueous phenol. Two glycophorins, designated glycophorins HA and HB, were isolated by two different techniques: preparative gel electrophoresis in the presence of sodium dodecyl sulfate and ion-exchange chromatography in the presence of the nonionic detergent Ammonyx LO. Each glycophorin formed at least two bands on gel electrophoresis, which corresponded to a dimeric form and a monomeric form. Glycophorin HA, the major component, had a blocked amino-terminus an...
Effect of pyrrolizidine alkaloid-induced hepatic disease on plasma amino acid patterns in the horse.
American journal of veterinary research    November 1, 1980   Volume 41, Issue 11 1894-1898 
Gulick BA, Liu IK, Qualls CW, Gribble DH, Rogers QR.Plasma amino acid patterns were studied in 6 clinically normal adult horses during the course of hepatic disease induced by feeding them plants containing pyrrolizidine alkaloids. At death, there were significant (P less than 0.01) increases in glutamine, proline, tyrosine, asparagine, lysine, histidine, alanine, phenylalanine, methionine, aspartic acid, and ornithine values. There were no significant changes in glycine, valine, isoleucine tryptophan, and arginine values. There were significant (P less than 0.01) decreases in citrulline. Ammonia increased 4-fold. Alpha-Aminoadipic acid and alp...
Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms.
The Journal of biological chemistry    October 10, 1980   Volume 255, Issue 19 9196-9204 
Jabusch JR, Bray RP, Deutsch HF.the sequence of the low activity form of equine erythrocyte carbonic anhydrase has been determined. The most common electrophoretic form, designated D, has been found to have five substitutions. Amino acid exchanges in the electrophoretic variants known as A1, A2, B, and T have been found at six other positions. The data do not permit calculation of the number of polymorphic forms of this enzyme. The equine D isozyme and the analogous human enzyme are quite homologous, 211 of their 260 residues, or 81%, being identical.
[Hemoglobins, XXXIII. Note on the Sequence of the hemoglobins of the horse (author’s transl)].
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    July 1, 1980   Volume 361, Issue 7 1107-1116 
Matsuda G, Maita T, Braunitzer G, Schrank B.The sequence analysis of the slow migrating component of the hemoglobins of horse was repeated with the automatic methode in the sequenator and the sequence of the beta-chains completed. In the alpha-chains the positions of alpha63 and alpha65 (Gly, Ala) and alpha82 and alpha85 (amides) were changed and the remaining 40 sequences of the beta-chains are reported. According to these data and biological contributions of other authors, the biological aspects of the primary structure and the polymorphism of the hemoglobins of the horse are discussed.
Purification and characterization of donkey chorionic gonadotrophin.
The Journal of endocrinology    June 1, 1980   Volume 85, Issue 3 449-455 doi: 10.1677/joe.0.0850449
Aggarwal BB, Farmer SW, Papkoff H, Stewart F, Allen WR.Serum of the pregnant donkey, like that of the mare, contains a gonadotrophin of chorionic origin. The chorionic gonaditrophin of the donkey (dCG) has been isolated in purified form from the serum of pregnant donkeys using methodology previously employed for the purification of pregnant mare chorionic gonadotrophin (eCG). Unlike eCG, dCG is predominatly an LH in biological tests. In the in-vitro rat Leydig cell assay, dCG was as active as eCG, but in the in-vitro rat seminiferous tubule assay for FSH and in the augmentation assay, dCG was considerably less potent than eCG (1-10%). Specific rat...
In vitro fermentation of feces from normal and chronically diarrheal horses.
American journal of veterinary research    April 1, 1980   Volume 41, Issue 4 564-567 
Minder HP, Merritt AM, Chalupa W.Feces from 13 healthy horses and 8 horses with chronic diarrhea were subjected to an in vetro fermentation procedure that had been developed for rumen fluid. Fermentations were conducted over 6 hours in a closed system, with and without an essential amino acid (EAA) mixture being added to the basic starch-buffer medium. The addition of EAA caused no significant difference in results of fermentation of feces from healthy horses. For diarrheic animals, there was a significant (P less than 0.01) increase in gas and total volatile fatty acids production whether EAA were present or not, and alpha-a...
Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c.
Biochemistry    March 18, 1980   Volume 19, Issue 6 1117-1120 doi: 10.1021/bi00547a012
Smith HT, Millett F.Spectrophotometric titrations of five singly modified horse heart ferricytochromes c, specifically (trifluoromethyl)phenylcarbamylated (CF3PhNHCO-) or trifluoroacetylated (CF3CO-) at lysines-13, -72, and -79, were carried out. The CF3PhNHCO-Lys-13, Lys-79, and CF3CO-Lys-79 derivatives all underwent alkaline isomerization with loss of the 695-nm band to low-spin species with an apparent pK of about 8.9, as did the unmodified cytochrome. However, modification of lysine-72 appeared to alter the reaction pathway since the CF3PhNHCO-Lys-72 derivative isomerized to a high-spin form with an apparent ...
Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism.
Biochemistry    February 19, 1980   Volume 19, Issue 4 743-750 doi: 10.1021/bi00545a021
Verheij HM, Volwerk JJ, Jansen EH, Puyk WC, Dijkstra BW, Drenth J, de Haas GH.It is known that His-48 is part of the active center in pancreatic phospholipase. To further elucidate the role of histidine-48 in the active center of pancreatic phospholipase A2, we have modified the enzyme with a number of bromo ketones and methyl benzenesulfonates. Rapid methylation occurred with methyl p-nitrobenzenesulfonate. Methylated phospholipase shows total loss of enzymatic activity whereas binding of substrate and the cofactor Ca2+ remains intact. Amino acid analysis of methylated equine phospholipase showed the loss of the single molecule of histidine and the formation of one mol...
A new method for the isolation of aminoacylase from mammalian kidneys.
Acta biochimica et biophysica; Academiae Scientiarum Hungaricae    January 1, 1980   Volume 15, Issue 4 287-293 
Szajáni B.Aminoacylase (E.C. 3.5.1.14) was isolated from the kidneys of different mammalian species (horse, cattle, rabbit and pig) by extracting the organ with water and subjecting the extract to heat treatment at 70 degrees C for 10 min, then, after having removed denatured proteins by fractionating those remaining in the solution by ammonium sulfate. The enzyme obtained in this way can either be used directly for practical purposes (e.g. preparation of immobilized aminoacylase) or further purified by chromatography. For the further purification of porcine kidney aminoacylase we applied a combination ...
Lymphocyte specificity to protein antigens. II. Fine specificity of T-cell activation with cytochrome c and derived peptides as antigenic probes.
The Journal of experimental medicine    February 1, 1979   Volume 149, Issue 2 436-447 doi: 10.1084/jem.149.2.436
Corradin G, Chiller JM.Murine T-lymphocyte specificity was determined in a system of antigen driven in vitro T-cell proliferation using cytochrome c molecules from different species, their derived peptides and reconstituted hybrid proteins. It was observed that primed T cells could discriminate between peptide fragments which differed from each other at a single amino acid residue. These conclusions were substantiated by the pattern of cross-reactivity noted in the response of closely related cytochrome c proteins as well as when artificial hybrid molecules reconstituted by the covalent linkage of peptide fragments ...
Purification of horse renal kallikrein and chemical relations with horse urinary kallikrein.
Advances in experimental medicine and biology    January 1, 1979   Volume 120A 325-333 doi: 10.1007/978-1-4757-0926-1_31
Porcelli G, Marini-Bettolo GB, Croxatto HR, Di Jorio M.Kallikrein was purified from horse kidney by several steps of chromatographic procedure and by affinity chromatography on Sepharose-Concanavaline. Horse urinary kallikrein was previously purified by DE-32 hydroxylapatite and by Sephadex G-100 gel filtration. On the purified final sample of renal and urinary kallikrein the aminoacid composition and the gel electrophoretic molecular weight were determined. The ratio in micronMoles between each aminoacid residue of both hydrolyzed renal and urinary kallikrein of horse is about 1,00 +/- 0,30. Except for Pro, 1/2 Cys and basic aminoacid residues a ...
Amino acid sequence of the beta-subunit of the follicle-stimulating hormone from equine pituitary glands.
The Journal of biological chemistry    August 10, 1978   Volume 253, Issue 15 5363-5368 
Fujiki Y, Rathnam P, Saxena BB.A tentative amino acid sequence of the beta-subunit of equine follicle-stimulating hormone (FSH) was derived from the sequences of tryptic, thermolytic as well as peptic, subtilisin, and chymotryptic peptides. Equine FSH-beta is analogous to human FSH-beta except six amino acid substitutions at positions 12, 16, 21, 62, 108, and 114. The amino acid sequence suggests that the hormone-specific beta-subunits of FSH are similar at the interspecies level, whereas the amino acid sequences of the hormone nonspecific alpha-subunits show variations.
[The interaction between phosphate and protein, and the respiration of the llama, the human fetus and the horse (author’s transl)].
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    May 1, 1978   Volume 359, Issue 5 547-558 
Braunitzer G, Schrank B, Stangl A, Bauer C.The sequence analysis of llama (Lama glama, Camelidae) hemoglobin is described. The chains were separated, cleaved by trypsin as previously described, quantitatively characterized and sequenced in the sequenator. The llama hemoglobin differs from the human hemoglobin in that it has 25 different amino acids in the alpha chain and 24 different amino acids in the beta chain. The interaction between protein and phosphate is discussed. The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, ...