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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.
Crystallization and properties of creatine kinase from equine skeletal muscle. 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. 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. 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 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)]. 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. 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. 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. 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. 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. 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. 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. 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. 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)]. 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, ...
Physicochemical and biological characterizations of pregnant mare serum gonadotropin and its subunits. Pregnant mare serum gonadotropin and its subunits have been further characterized. Ultracentrifugation of the gonadotropin at pH 1.3 and 11.5 showed little evidence of dissociation compared to pH 8.2. Highly purified subunits are obtained by urea dissociation and ion-exchange chromatography followed by gel-filtration. Circular dichroism spectra of the gonadotropin and its subunits are much like those of ovine lutropin and its subunits in that there is little evidence for secondary structure and one or more tyrosine residues are inaccessible in the intact gonadotropin compared to the subunits. ...
Response to dietary nitrogen in ponies. Utilisation of nitrogen was studied in 4 crossbred ponies. A latin square design was used to study the effects of corn gluten meal, casein or urea when added to a low protein basal diet. Apparent nitrogen digestion, nitrogen retention, total plasma protein, plasma urea and plasma-free amino acids were measured. The addition of corn gluten meal, casein or urea to the basal ration increased apparent digestion of nitrogen. Casein produced a significantly greater (P less than 0.05) nitrogen retention than corn gluten meal or urea. Plasma urea nitrogen increased significantly (P less than 0.01) in ...
Analysis of a complex antigenic site on horse cytochrome c. Of the antigenic determinants so far identified for cytochrome c, only one involves more than a single amino acid substitution between the immunogen and host proteins. Both a threonine at position 89 and a glutamic acid at position 92 control one of the three antigenic sites identified in horse cytochrome c, as expressed in rabbits. Three antibody subpopulations, all directed against this region of the molecule, were isolated from the serum of a single rabbit by adsorption on a series of insolubilized cytochromes c. Antibody fluorescence quenching titrations with a variety of cytochromes c wer...
Phenylalanine inhibited p-nitrophenyl phosphatase activity in the serum as an indication of intestinal cellular disruption in the horse. Examination of tissues obtained from thoroughbred horses showed that the 'intestinal' phosphatase activity could be differentiated from other phosphatases by analysis at a pH of 9-5 and inhibition with 15 mM L-phenylalanine. A simple method for the measurement of 'intestinal' phosphatase in heparinised plasma or serum is described. Application of the technique to serum or plasma from normal and diseased horses indicates that the increase in the activity of 'intestinal' phosphatase is associated with cases showing clinical, biochemical and haematological evidence of intestinal damage.
Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice. Two phospholipases A2 (EC 3.1.1.4) with different isoelectric points have been isolated from horse pancreas in high yield (880 mg/kg tissue). From pancreatic juice the more acidic species was isolated as the sole phospholipase A2. Upon tryptic activation the zymogens release a hepta- and pentapeptide, respectively from the N-terminal part of the protein giving rise to the formation of one single enzyme with a specific activity higher than that of pancreatic phospholipases A2 from other mammalian species. Horse phospholipase A2 differs from the porcine and bovine enzymes with respect to amino a...
Amino acid sequence of phospholipase A2 from horse pancreas. The complete amino acid sequence of phosphlipase A2 (EC 3.1.1.4) from horse pancreas was determined. The protein controls of a single polypeptide chain of 125 amino acids and has a molecular weight of 13,927. The chain is crosslinked by seven disulfide bridges. The sequence was determined by automated Edman degradation of the intact protein and several of the large peptide fragments. Smaller peptides were analyzed by manual Edman degradation. Fragmentation of the peptide chain was accomplished by enzymatic digestion with trypsin, chymotrypsin, and thermolysin. The final overlap was found by di...
Guanidination of horse methemoglobin. Reaction of horse methemoglobin with O-methylisourea at pH 10.2 results in 95% conversion of lysine residues to homoarginine. Analysis of the chymotryptic peptides showed that no single ϵ-amino group was unreactive. Guanidination decreases the dependence of the sedimentation coefficient on hydrogen ion concentration in the range of pH 8 to 11 and did not affect the dependence on protein concentration at pH 7. These results support the conclusion that the lysine side chains involved in subunit contacts have sufficient freedom to accommodate the small changes in bulk and geometry associated wit...
Amino acid composition of casein isolated from the milks of different species. Casein was isolated from the milks of the following species: cow, horse, pig, reindeer, caribou, moose, harp seal, musk-ox, polar bear, dall sheep, and fin whale. The caseins were subjected to acid hydrolysis, the resultant amino acids were converted to their n-butyl-N-trifluoroacetyl esters, and the amino acid composition of the caseins was determined by gas chromatographic analysis of these esters. Notable among the results was the close similarity, with respect to amino acid composition, of reindeer and caribou caseins. The results of the amino acid analyses of the other caseins are present...
Amino-acid sequence of equine renal metallothionein-1B. The amino-acid sequence of a metallothionein is reported. Metallothionein is a widely distributed, extremely cysteine-rich, low-molecular-weight protein containing large amounts of cadmium and/or zinc. Metallothionein-1B is one of the two prinicipal variants occurring in equine kidney cortex. The single-chain protein contains 61 amino acids and has the composition Cys20 Ser8Lys7Arg1Ala7Gly5Val3Asp2Asn1-Glu1Gln2Pro2Thr1Met1(Cd + Zn)7. Its amino-terminal residue is N-acetylmethionine. The sequence shows distinct clustering of the twenty cysteinyl residues into seven groups separated by stretches...
Utilization of proteins by the equine species. Protein digestion, nitrogen retention, plasma protein, plasma urea, and plasma-free amino acids were determined for ponies fed 3 different protein supplements. Substitution of casein, corn gluten meal, or corn gluten meal plus lysine for a portion of the cornstarch in a low-protein basal ration increased apparent digestion of protein. Substitution with either casein or corn gluten meal plus lysine produced a significant increase (P less than 0.05) in nitrogen retention, whereas the corn gluten meal substitution did not. Nitrogen retention, expressed as percentage of nitrogen absorbed, was incr...
Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with diazonium-1H-tetrazole. Diazonium-1H-tetrazole was tested as a potential active-site-directed reagent for amino acid residues involved in catalysis by alcohol dehydrogenase. In a novel reaction with a protein, diazonium-1H-tetrazole inactivated the enzyme selectively, and almost stoichiometrically, but reacting with the sulfur of a cysteine residue, Cys-174. As a model compound, the tetrazole adduct of free cysteine was prepared. Elementary and spectral analyses of the adduct were consistent with the structure 5-tetrazoleazo-S-cysteine. The adduct absorbs light with a maximun at 316 nm, and is destroyed by irradiatio...
Characterization of human, bovine, and horse antithrombin III. A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single poly...
Purification, characterization, and quantitation of the antigen employed in the immunodiffusion test for diagnosis of equine infectious anemia. Equine infectious anemia (EIA) antigen extracted from the spleen of horses infected with EIA virus was purified by pH treatment, (NH4)2SO4 fractionation and affinity chromatography. The homogeneity of the antigen was indicated by sedimentation rate and sedimentation equilibrium experiments. A S20,w of 0.51 was determined and a molecular weight of 7600 was calculated from sedimentation equilibrium analysis. The amino acid composition of the pure antigen indicated the antigen is an acidic protein. Employing radical immunodiffusion (RID) and pure antigen a method for quantitating antigen content ...
Isolation and partial characterization of three major allergens of horse hair and dandruff. Three major allergens of horse hair and dandruff have been isolated. The fractionation procedures involved various combinations, described in detail, of ethanol precipitation below --5degreesC, cation- and anion-exchange chromatography, and gel filtration. UV absorption, quantitative immunoelectrophoresis and RAST inhibition were used to monitor the separations. Protein impurities constituted less than 5% in all cases. The molecular weights of the isolated proteins were 1.9 X 10(4), 5.1 X 10(4) and 3.1 X 10(4) daltons, respectively. The pIs were determined as 4.1, 3.8 and 3.9, respectively. Th...
N-acetylserine in horse muscle acylphosphatase. A ninhydrin-negative peptide fraction obtained from tryptic digest of carboxymethyl acylphosphatase was isolated by chromatography on a column of PA 28 Beckman resin and analysed for the amino acid composition. Degradation with carboxypeptidase B and A indicated that the sequence of this peptide was: X-Thr-Ala-Arg. The amino-terminal residue was identified as N-acetylserine by high voltage electrophoresis. It is therefore suggested that the sequence of the NH2-terminal portion of CM-acylphosphatase is N-acetyl-Ser-Thr-Ala-Arg. Digestion with carboxypeptidase A and B indicated also that the COO...
