Topic:Amino Acid Sequence
Amino acid sequences in horses refer to the specific order of amino acids in a protein, which is crucial for determining the protein's structure and function. These sequences are encoded by the horse's genetic material and are essential for various biological processes, including muscle development, enzyme activity, and immune response. Understanding amino acid sequences in horses can provide insights into genetic diseases, performance traits, and overall health. This topic explores the latest research on equine amino acid sequences, focusing on their role in protein synthesis, genetic variation, and implications for breeding and veterinary medicine. The page compiles peer-reviewed studies and scholarly articles that investigate the significance of amino acid sequences in equine biology.
Structure of horse-muscle phosphoglycerate kinase at 6 angstrom resolution. The single peptide chain of 3-phosphoglycerate kinase is folded into two distinct globular units, only one of which seems to be involved in substrate binding.
N-Terminal sequences of equine and human immunoglobulin heavy chains. N-terminal tetrapeptides from heavy chains of equine γGab- and γT-globulins, and of human γG and γA myeloma proteins and a γM macroglobulin, have been studied. The equine and human heavy chains lacked free α-amino-terminal groups. After mild alkaline hydrolysis, glutamic acid was identified as the terminal amino acid by reaction with dimethylaminonaphthalenesulfonyl chloride, tentatively identifying pyrrolid-2-one-5-carboxylic acid (PCA) as the unreactive terminal residue of each heavy chain. Peptides lacking a free α-amino group were isolated from subtilisin and pronase digests of the ...
A comparison of fingerprints of tryptic digests of human, horse and rat apoferritins. 1. Fingerprints of tryptic digests of apoferritins from a human liver, horse spleens and ACI rat livers were made by means of electrophoresis and chromatography on microcrystalline cellulose, and were compared.
2. All tryptic peptides also present in apoferritins from the human liver and the horse spleens were also present in apoferritin from the rat livers.
3. In the digests of horse and of rat apoferritin there was a peptide that was not present in the digests of human apoferritin. Another peptide was obtained from human and from rat apoferritin, but not from horse apoferritin.
4. T...
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.
Equine antihapten antibody. The subunits and fragments of anti-beta-lactoside antibody. Eight antigenically unique immunoglobulins have been identified in purified equine anti-p-azophenyl-beta-lactoside (Lac) antibody isolated from a single horse. The Fc fragments of the gammaGa-, gammaGb-, gammaGc-, and -gammaA-globulins have been shown to possess unique antigenic determinants. Common gammaG- and gammaA-Fc fragment antigenic determinants, which were absent from the 10Sgamma(1)- and gammaM-globulins, have also been observed. All antibody populations share two antigenically distinct light (B, L) chain variants. The association of anti-Lac antibody with the hapten p-(p-dimethylamin...