Omneity® Pellets
All-In-One Vitamin & Mineral Pellet
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.
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.
Isolation and amino acid sequence of the alpha-subunit of follicle-stimulating hormone from equine pituitary glands. Six hundred milligrams of follicle-stimulating hormone (FSH), containing 110 NIH-FSH-S1 units/mg, was isolated from 9 kg of equine pituitary glands. The equine FSH was dissociated into alpha- and beta-subunits. A tentative amino acid sequence of the alpha-subunit was determined. The alpha-subunit contained 82 amino acids. The equine FSH-alpha is shorter by 10 to 14 amino acids at the NH2 terminus and has several substitutions at several positions as compared with human FSH-alpha and bovine thyroid-stimulating hormone-alpha. At the intraspecies level, the alpha-subunits of human FSH, human lute...
[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, ...
Biochemical changes in horses during a 50-mile endurance ride. Blood samples were taken from 15 horses before and after a 50-mile ride to examine the changes occurring in some biochemical constituents. There was a significant (P less than 0.05) decrease in plasma potassium, calcium and magnesium concentrations and a rise in inorganic phosphate but there was no alteration in plasma sodium, chloride or protein levels or change in haematocrit. After the ride there was a highly significant (P less than 0.01) fall in blood glucose corresponding with increased lipolysis and a rise in plasma free fatty acids (P less than 0.001) and glycerol (P less than 0.001). ...
Specific reaction of aloe extract with serum proteins of various animals. We found that aloe extract contains a lectin-like substance which reacts with serum proteins of various animals. Furthermore, in human serum 2 proteins, alpha2-macroglobulin and alpha1-antitrypsin, were shown to be reactive with aloe extract.
Circular dichroic properties and conformation of thionicotinamide dinucleotides bound to horse-liver alcohol dehydrogenase. The interaction between horse liver alcohol dehydrogenase and the oxidized and reduced forms of the 3-thionicotinamide--adenine dinucleotide coenzyme analogues (sNAD and sNADH) has been investigated by ultraviolet absorption, fluorescence and circular dichroism. The fluorescence of sNADH is enhanced when bound to the enzyme, and the protein fluorescence is quenched by both sNADH (60--65%) and sNAD (65%). The possible origin of the larger quenching produced by sNAD with respect to that of NAD is discussed. Coenzyme dissociation constants have been determined by monitoring the quenching of the p...
[Immunochemical investigations on the gene expression of horse serum carboxylesterase (author’s transl)]. Immunochemical and enzymatic analyses of horse serum carboxylesterase were carried out with respect to the existence of a silent gene. Sera with positive phenotypic expression of esterase, both heterozygotes and presumed homozygotes, were compared with:--sera with positive phenotypic expression but genotypically +/O;--sera with a negative phenotypic expression, i. e. genotypically O/O;--sera of natural +/O "hemi-zygotes": mules (donkey lacking the esterase);--positive sera heated at 60 degrees C;--positive sera after specific inhibition of enzymatic activity. Titration by immunocompetition has...
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. ...
Stability and kinetic behavior of carboxymethylated horse muscle acylphosphatase. Horse muscle acylphosphatase consists of a main chain S-S bound to glutathione. It was found that removal of the glutathione by reduction and successive carboxymethylation of the only cysteine of the main chain affects the stability of the enzyme, mainly with respect to thermal inactivation. On the other hand, the kinetic properties of the enzyme are affected very little.
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 ...
Polymorphic post-albumin of cattle and horse plasma identified as vitamin D binding protein (Gc protein). Cattle and horse plasma samples of known post-albumin types were radiolabelled with 14C-vitamin D3. These samples were then analysed by polyacrylamide gel electrophoresis, followed by autoradiography. The patterns observed were identical to those of post-albumin variants. The polymorphic post-albumin protein of cattle and horse was thus identified as the vitamin D binding protein and homologous to the Gc protein of human plasma.
Genetic polymorphism of the vitamin D binding protein and another post-albumin protein in horse serum. Horizontal polyacrylamide gel electrophoreses, on 10% separation gel, of horse serum revealed polymorphism of the vitamin D binding protein (Gc protein) and another post-albumin protein (Pa). Family data supported the hypothesis that Gc and Pa types were controlled by autosomal codominant alleles. For both Gc and Pa proteins, the homozygous types showed a single fraction while the heterozygous type had two fractions. Pa types were found to be identical to the post-albumin types reported earlier by starch gel electrophoresis. Two Gc alleles, GcF and GcS, and three Pa alleles, Pa D, Pa F and Pa ...
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...
Somatostatin-containing cells in the rat and horse pancreatic islets. Somatostatin-, glucagon- and insulin-containing cells in the rat and horse pancreatic islets were investigated by an indirect immunofluorescent technique using antibodies to insulin, glucagon and somatostatin. In the rat pancreatic islets, insulin-containing cells were located centrally, and glucagon and somatostatin or somatostatin-like substance (SLS)-containing cells were peripherally disposed and glucagon-containing cells were situated more peripherally as compared with distribution of somatostatin-containing cells. On the other hand, in the horse pancreatic islets, insulin-containing cell...
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c. Iodination of horse cytochrome c with the lactoperoxidase-hydrogen peroxide-iodide system results initially in the formation of the monoiodotyrosyl 74 derivative. This singly modified protein was obtained in pure form by ion exchange chromatography and preparative column electrophoresis. It shows an intact 695 nm absorption band, the midpoint potential of the native protein, a nuclear magnetic resonance spectrum which indicates an undisturbed heme crevice structure, a normal reaction with antibodies directed against native horse cytochrome c, and circular dichroic spectra in which the only cha...
A subunit-sized butyrylcholinesterase present in high concentrations in pooled rabbit serum. A butyrylcholinesterase of mol.wt. approx. 83000 was observed in pooled rabbit serum. The enzyme was named monomeric butyrylcholinesterase to distinguish it from the larger oligomeric butyrylcholinesterase of horse and human serum whose subunits are the same size as the monomeric enzyme. The active-site concentration of monomeric butyrylcholinesterase in the pooled serum was 0.18mum, which is five times the concentration of butyrylcholinesterase in pooled horse serum. This was surprising, since the horse serum is regarded as a rich source of butyrylcholinesterase, whereas rabbit serum is not g...
Circular dichroism of porcine, bovine, and equine pancreatic phospholipases A2 and their zymogens. Unusual conformations simulating helix content. Conformation of porcine, bovine, and equine pancreatic phospholipases A2 (EC 3.1.1.4) and their zymogens was studied by the circular dichroism (CD) probe in the far and near ultraviolet spectral zones.
All these phospholipases and their zymogens displayed CD curves suggesting the presence of moderate amounts of α-helical conformation. However, on the basis of known primary structure and recent X-ray structural analysis of prophospholipase A2 crystals (Drenth, J., Enzing, C.M., Kalk, K.H. and Vessies, J.C.A. (1976) Nature 264, 373–377), it has to be concluded that the positive CD band cen...
Semisynthetic cytochrome c. Horse heart cytochrome c can be split with cyanogen bromide into a heme peptide (residues 1-65) and a nonheme peptide (residues 66-104). In a process involving (i) complex formation between the two fragments and (ii) restoration of the severed peptide linkage, a fully active cytochrome c preparation can be re-formed. Use has been made of this process to couple the heme peptide to peptide 66-104 synthesized by the Merrifield solid-phase procedure. The semisynthetic product formed in this manner is indistinguishable from reconstituted cytochrome c prepared with nonsynthetic peptide 66-104.
Characterization of a retravirus isolated from squirrel monkeys. A new retravirus (SMRV) isolated from a squirrel monkey, Saimiri sciureus, has an Mg2+-dependen reverse transcriptase and a buoyant density of 1.17 g/cm3 in sucrose and 1.21 g/cm3 in cesium chloride, similar to the mouse mammary tumor virus and the Mason-Pfizer monkey virus. The polypeptide patter of SMRV as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was distinct from the reported polypeptide patterns of known retraviruses. Four major polypeptides of molecular weights 40,000, 20,000, 14,000 and 8,000 were resolved in virus propagated in human, mink, and canine cell...
The oxidation of ferrocytochrome c in nonbinding buffer. The apparent equilibrium constant and rate of oxidation was investigated for the reaction of cytochrome c with iron hexacyanide. It was found that if horse heart ferricytochrome c was exposed to ferricyanide (to oxidize traces of reduced protein) the cytochrome subsequently, even after extensive dialysis, had an apparent equilibrium constant different from that of electrodialyzed protein. The effect of ferricyanide ion apparently cannot be removed by ordinary dialysis. The ionic strength dependence of the apparent equilibrium constant and bimolecular oxidation rate constant was measured in the...
Electronic and steric factors affecting ligand binding: horse hemoglobins containing 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme. Horse globin has been recombined with 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme to yield the corresponding reconstituted hemoglobins, and the ligand binding reactions of these reconstituted hemoglobins have been examined in detail. Both hemoglobins exhibit relatively high n values, but 2,4-dimethyldeuterohemoglobin displays a consistently higher oxygen affinity than native hemoglobin, whereas the oxygen affinity of 2,4-dibromodeuterohemoglobin is consistently lower than that of native hemoglobin. The rate constants l’, and 1’4 for the binding of the first and fourth molecules of C...
Equine angiotensin converting enzyme: a zinc metalloenzyme. 1. Angiotensin I converting enzyme from horse plasma has been extensively purified and shown to be homogeneous by disc-gel electrophoresis. 2. The metal ion involved in the catalytic reaction of the enzyme has been identified for the first time as zinc by atomic absorption spectrometry. 3. A number of other physicochemical properties of the enzyme are described and compared with results obtained by other investigators. The molecular weight was determined by gel filtration to be 113 000 daltons. The pH maximum was found to be 7-4. The chloride activation of the enzyme appears to act by facilita...
