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.
Small intestinal beta-galactosidase activity in the horse. Two enzymes having lactase activity are present in the equine small intestine. The first, the digestive enzyme, neutral beta-galactosidase, declines in activity from birth to three years, disappearing completely between 3 and 4 years of age. The other, the soluble lysosomal enzyme, acid beta-galactosidase, having affinity for lactose and a synthetic beta-galactoside, shows a decrease in activity in the first three months of life and thereafter varies little in activity and represents the lactase enzyme in the adult horse. This pattern may parallel the development of lactase activity in many ot...
Studies on the metabolism of sympathomimetic amines. The metabolism of (plus or minus)-(14C)noradrenaline in the horse. 1. The metabolism of (±)-[14C]noradrenaline in horses has been studied. The plasma half-life of radioactivity following intravenous injection was 95 min.
2. Two horses each excreted about 80–85% of the radioactivity in the urine in 15 h after rapid intravenous injection and about 75% of the excreted radioactivity has been identified.
3. The unchanged drug in the urine accounted for less than 1% of the dose and 3-methoxynoradrenaline for about 7%. The main metabolites were 4-hydroxy-3-methoxymandelic acid (22%), 4-hydroxy-3-methoxybenzoic acid (13%) and 4-hydroxy-3-methoxyphenylglycol ...
The biochemistry of ferritin. The researchers investigated the biochemical properties of ferritin, a protein responsible for iron storage in the body. They identified its distribution and structure, noting variations in different species and tissues. […]
Reduction of ferricytochrome c by dithionite ion: electron transfer by parallel adjacent and remote pathways. The kinetics of the reduction of horseheart ferricytochrome c by sodium dithionite (phosphate buffer-sodium chloride; pH 6.5, mu = 1.0, 25 degrees ) features two reaction pathways; one with the rate constant k(3) = 1.17 x 10(4) M(-1) sec(-1), the other with the rate constant k(1)k(2)/k(-1) = 6.0 x 10(4) M(-1) sec(-1). These pathways are interpreted in terms of remote attack (possibly by way of the exposed edge of the porphyrin system) and adjacent attack (requiring the opening of the heme crevice). The limiting rate for the adjacent pathway (k(1) = 30 sec(-1)) is in good agreement with the rat...
Extraction of equine infectious anemia immunodiffusion antigen with the aid of the chaotropic agent, thiocyanate. Immunodiffusion antigen from spleens of horses infected with equine infectious anemia virus was prepared by methods employing freeze-thaw cycles and thiocyanate treatment. Thiocyanate (0.5 M) permitted the recovery of the greatest amount of antigen. Furthermore, it was most effective for recovery of immunodiffusion antigen from spleens which yielded unsatisfactory concentrations of antigen by the conventional freeze-thaw or water-extraction methods. The reactivity of the antigen did not appear to be affected by this chemical treatment.
Intermicrosomal distribution of aromatizing enzyme system in equine testicular tissue. The microsomal fraction (10 000–105 000 × g precipitate) of equine testes was fractionated into the smooth- and the rough-surfaced microsomal subfractions by a sucrose density-gradient centrifugation in the presence of CsCl. The validity of this fractionating procedure was confirmed by electron microscopic examination and also by chemical analysis of the RNA contents in these subfractions. The aromatizing enzyme system (19-hydroxylase and aromatase) which was concentrated in the microsomal fractions among the organellae was found to be localized in the smoothsurfaced microsomal fraction. Th...