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Topic:Proteomics

Proteomics is the large-scale study of proteins, particularly their structures and functions, in horses. This field encompasses the analysis of the complete set of proteins expressed by the equine genome, known as the proteome. Proteomics research in horses aims to understand the diverse roles of proteins in various biological processes, including growth, development, and response to environmental stimuli. Techniques such as mass spectrometry and protein microarrays are commonly employed to identify and quantify proteins, assess post-translational modifications, and investigate protein-protein interactions. This page compiles peer-reviewed research studies and scholarly articles that explore the methodologies, findings, and implications of proteomics in equine health and disease.
Comparative studies on the soluble protein fractions of bovine, equine, porcine and ovine adrenal chromaffin granules.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 6C-7C doi: 10.1042/bj1000006c
Helle KB.No abstract available.
[Study of some oligopeptides isolated from chymotrypsin hydrolysates of horse myoglobin globin].
Bulletin de la Societe de chimie biologique    January 1, 1966   Volume 48, Issue 5 733-735 
Boulanger Y, Dautrevaux M, Han KK, Biserte G.No abstract available
[Study of the “median” peptide freed from horse myoglobin by cyanogen bromide].
Bulletin de la Societe de chimie biologique    January 1, 1966   Volume 48, Issue 8 995-997 
Han K, Dautrevaux M, Boulanger Y, Biserte G.No abstract available
Proteolysis of salmine by horse urinary kallikrein.
Biochemical pharmacology    November 1, 1965   Volume 14, Issue 11 1665-1671 doi: 10.1016/0006-2952(65)90021-3
Brandi CM, Mendes J, Paiva AC, Prado ES.No abstract available
The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin.
The Biochemical journal    September 1, 1965   Volume 96, Issue 3 693-699 doi: 10.1042/bj0960693
Black JA, Leaf G.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...
[Studies of the N-Terminal Amino Acid Sequence in the Serum Albumins of Different Animals].
Biokhimiia (Moscow, Russia)    July 1, 1964   Volume 29 741-748 
ORLOVSKAIA NN, BELITSER VA.No abstract available
The Submolar Quantities of N-Terminals in Proteins: Effect of Sodium Dodecyl Sulfate on the N-Terminals of Egg Albumin and Bovine, Equine, and Porcine Gamma-Globulins.
Archives of biochemistry and biophysics    January 1, 1964   Volume 104 27-31 doi: 10.1016/s0003-9861(64)80030-8
COLACICCO G.No abstract available
The application of Edman’s peptide degradation method to horse myoglobin and haemoglobin.
Biochimica et biophysica acta    April 1, 1955   Volume 16, Issue 4 599-600 doi: 10.1016/0006-3002(55)90290-0
INGRAM VM.No abstract available
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