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.
Specific hemagglutinin and a modulator of complement in cockroach hemolymph. Natural hemagglutinin activity against vertebrate erythrocytes is present in the hemolymph of the cockroach Blabarus craniifer. The hemagglutinin titer against rabbit erythrocytes is high, whereas sheep and horse red cells agglutinate weakly. Hemagglutinin activity was depressed by the complement inhibitor, cobra venom factor. Cockroach hemagglutinin is heat-labile; all activity is destroyed by heating at 56 C for 1 hr. A humoral factor similar to the complement component 3 proactivator is also present in cockroach hemolymph. The formation of the cobra venom factor-hemolymph "complex" is depen...
Characterization of an equine infectious anemia antigen extracted from infected horse spleen tissue. The spleens of horses infected with equine infectious anemia contain an antigen that is useful for a diagnostic immunodiffusion test. This antigen was extracted from the spleen by homogenization of the tissue, centrifugation, and precipitation from the supernatant fluid at 50% saturation with (NH(4))(2)SO(4). The antigen was purified by subjecting it to two cycles of electrophoresis in a continuous free-flow electrophoresis cell and finally filtering through a column of Sephadex G-200 gel. The antigen was found to be a small protein with a molecular weight of 27,500 and sedimentation coefficie...
Formation of estrogens by the pregnant mare. II. Metabolism of 14C-acetate and 3H-cholesterol injected into the fetal circulation. A mixture of 14C-sodium acetate and 3H-cholesterol was injected into the umbilical circulation of a pregnant mare in the 3OOth day of gestation. The abdomen was closed and urine was collected for 3.5 days. The mare delivered a normal live foal 23 days later. Steroid conjugates present in the maternal urine were hydrolyzed and separated into neutral and phenolic fractions. From the phenolic “sulfate” fraction estrone, 17α-estradiol, equilin, equilenin, and 17α-dihydroequilenin were isolated. Only estrone and 17α-estradiol contained both 3H and 14C, while the ring-B unsaturated estrogens ...
Studies on the IgA system of the horse. Equine serum and secretions were found to contain a protein which cross-reacted with an antiserum against human IgA, but not with antisera against any other human immunoglobulin. The physicochemical properties of equine IgA resembled those of human IgA. IgA was found to be the immunoglobulin having the highest secretion serum concentration ratio in equine lacteal and salivary secretions, and to be the protein produced by the majority of immunoglobulin-containing cells in the of the equine intestine.
Kallidin (lysylbradykinin), the kinin formed from horse plasma by horse urinary kallikrein. Horse urinary kallikrein when incubated with horse plasma formed kallidin (lysylbradykinin) from the kininogens in the plasma. Horse plasma, like human plasma, was found to contain an aminopeptidase capable of converting kallidin to bradykinin. No evidence, however, could be found that the plasma contained an aminopeptidase capable of converting Met-Lys-bradykinin to kallidin, thus eliminating the possibility that the kallikrein had released Met-Lys-bradykinin which was converted to kallidin during the 1–5 min incubations. The method used for identification of the kinins is rapid, gives a go...
The binding of carbon dioxide by horse haemoglobin. 1. Three modified horse haemoglobins have been prepared: (i) alpha(c) (2)beta(c) (2), in which both the alpha-amino groups of the alpha- and beta-chains have reacted with cyanate, (ii) alpha(c) (2)beta(2), in which the alpha-amino groups of the alpha-chains have reacted with cyanate, and (iii) alpha(2)beta(c) (2), in which the two alpha-amino groups of the beta-chain have reacted with cyanate. 2. The values of n (the Hill constant) for alpha(c) (2)beta(c) (2), alpha(2)beta(c) (2) and alpha(c) (2)beta(2) were (respectively) 2.5, 2.0 and 2.6, indicating the presence of co-operative interactions ...