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.
Electron-microscopic and chemical studies of oligomers in horse ferritin. Horse ferritin was fractionated both by starch-gel electrophoresis and by gel filtration on Sephadex G-200. Monomer fractions contained up to 98% of monomer and oligomer fractions up to 76% of oligomers as determined by quantitative electron microscopy. Percentages obtained from electron micrographs correlated well with analytical starch-gel electrophoretograms and ultracentrifuge patterns. Amino acid analyses of monomer- and oligomer-enriched fractions showed no significant differences. Ferritin oligomers did not apparently dissociate on dilution for electron microscopy or on storage. Apoferr...
Amino acid sequences around the cystine residues in horse growth hormone. The cystine-containing peptides of horse growth hormone were isolated and their amino acid sequences determined. Four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus of the protein, 15 amino acids. These sequences are compared with published data on growth hormones from other species.
Comparison of the structure of the immunoglobulins from horse serum. A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is...
The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin. 1. The effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin have been investigated. Cytochrome c yielded four fragments, of which two were haemopeptides. The two colourless peptides had amino acid compositions corresponding to those that are expected, on the basis of the sequence proposed for horse-heart cytochrome c by Margoliash, Smith, Kreil & Tuppy (1961), from cleavage at both methionine residues. Of the two haemopeptides, one was isolated and shown to be that derived from cleavage at only one methionine residue, that nearer to the C-terminus of the peptid...
The amino acid contents of horse globin and of its component polypeptides. Horse globill and its conlponent polypeptide chains obtained by fractional
precipitation and column chroinatography have been ailalyzed for their con- stituent amino acids. The principal difference between the two chains is that
the valyl-leucyl chain is rich in serine and threonine and poor in glutamic acid
and tryptophan compared to the \-alyl-glutaininyl chain.
The oxidation of cystamine and homocystamine by mammalian enzymes. The oxidative deamination of cystamine and homocystamine by mammalian oxidases has been studied. The histaminase of pig kidney oxidizes homocystamine much more slowly than cystamine. The amine oxidase of mammalian liver (guinea-pig, rabbit) oxidizes homocystamine more rapidly than cystamine. Both amines are oxidized by plasma (or serum) of ruminants (ox, sheep, goat) and of the horse. In the enzymatic oxidation of homocystamine both aminogroups are removed; there is no evidence that a ring compound analogous to cystaldimine is accumulating.