Topic:Biochemistry
The study of biochemistry in horses encompasses the chemical processes and substances that occur within equine organisms. This field investigates the molecular interactions and pathways that are fundamental to horse physiology, including metabolism, enzyme activity, and genetic expression. Key areas of interest include the examination of metabolic disorders, nutrient absorption, and the biochemical basis of muscle function and energy production. Researchers utilize biochemical analysis to understand health and disease mechanisms in horses, contributing to the development of diagnostic tools and therapeutic strategies. This page gathers peer-reviewed studies and scholarly articles that explore various biochemical processes and their implications for equine health and performance.
Binding of long chain alkyl sulphates to equine ferric myoglobin. When ferric myoglobin reacts with alkyl sulphates, its absorption spectrum changes into one characteristic of a haemichrome or parahaematin. The reaction equilibrium was studied over a range of protein concentrations using dodecyl sulphate and other alkyl sulphates with different chain lengths. The results obtained from spectrophotometric measurements and equilibrium dialysis experiments are not in agreement with those of other authors who, from an analysis of spectral changes only, supported the hypothesis of an all-or-none type of reaction whereby 18 detergent anions were bound to one molecu...
Equine antihapten antibody. The molecular weights of the subunits of equine immunoglobulins. Three independent methods have been used
to determine the molecular weights of the heavyand light-polypeptide chain subunits of equine yGab-,
yGc-, and yT-immunoglobulins. Extensively reduced
and alkylated proteins were filtered through standard
columns of Sephadex G-100 or G-200 in 8 M urea405
M propionic acid. Subunit molecular weights were obtained from the linear elution volume, V,, us. logarithm
molecular weight relationship defined for each column
with rabbit yG-globulin heavy and light chains and
horse heart cytochrome c. Molecular weights also were
determined by equilibrium se...
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...