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.
A comparative study of blood gas tensions, oxygen affinity and red cell 2,3 DPG concentrations in foetal and maternal blood in the mare, cow and sow. 1. Blood gas tensions, pH, PCV, O(2) affinity and red cell 2,3-diphosphoglycerate (DPG) levels have been measured in uterine and umbilical blood in conscious cows and mares with indwelling vascular catheters and in sows under sodium pentobarbitone anaesthesia.2. Large P(O2) gradients (20-24 mmHg) were observed between the uterine and umbilical venous blood in the cow and pig, while in the mare the corresponding P(O2) difference was only 2.7 +/- 1.7 mmHg. Alterations in maternal arterial P(O2) did not affect the large vein-to-vein P(O2) difference in either ruminant or pig.3. In the cow the pre...
Photooxidation of horse and sperm-whale myoglobin sensitized by the heme group. The irradiation of horse and sperm-whale Fe” or Fez’ myoglobins with visible light
showed that axial ligands that render the heme diamagnetic (e.g. 02, CO or CN-) endow the
hemoproteins with a marked photosensitivity. In contrast, high-spin myoglobins are unaffected by
visible light. These findings appear to be of general validity for all hemo-proteins and are in agreement
with the involvment of the triplet state of the heme as the reactive intermediate. In all cases, the overall
photoprocess occurs within a very narrow spatial range, leading to specific modification of these
photoox...
A steady-state kinetic model of butyrylcholinesterase from horse plasma. The steady-state kinetics of the butyrylcholinesterase-catalysed hydrolysis of butyrylthiocholine and thiophenyl acetate were shown to deviate from Michaelis-Menten kinetics. The ;best' empirical rate law was selected by fitting different rate equations to the experimental data by non-linear regression methods. The results were analysed in view of two alternative interpretations: (1) the reaction is catalysed by a mixture of enzymes, or (2) the activity is due to a single enzyme displaying deviations from Michaelis-Menten kinetics. It was concluded that the second alternative applies, and this...
Cytochrome c: a thermodynamic study of the relationship among oxidation state, ion-binding and structural parameters. Cation binding to horse-heart ferrocytochrome c. The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel
filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability
constants are in the range of 5-8 mM-1, and the number of binding sites per protein molecule are
1 to 2. The temperature dependence of the stability constant for the Mg2+-ferrocytochrome system
was measured. The thermodynamic parameters were found to be: dH&s = 4-12 kcal/mol, dG;,,
(25 "C) = -5.6 kcal/mol and AS&, = +57 calxmol-lx K-I.
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand. Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the ...
Purification and antigenicity of an M-like protein of Streptococcus equi. A cell wall component of Streptococcus equi analogous to the M protein of group A streptococci has been identified and purified. A highly purified product has been obtained from cells by hot acid extraction, followed by acid precipitation, ammonium sulfate fractionation, and column chromatography. This product reacts with S. equi antiserum. The existence of this fraction in S. equi has been confirmed by the failure of trypsin-treated cells and their extracts to remove the long-chaining capacity of S. equi antiserum. The antigenicity of this M-like protein when incorporated in adjuvant has been...