Topic:Hemoglobin
Hemoglobin is an iron-containing protein found in the red blood cells of horses, responsible for the transport of oxygen from the lungs to the tissues and the return of carbon dioxide from the tissues to the lungs. It plays a vital role in maintaining cellular respiration and energy metabolism. The structure and function of hemoglobin can be influenced by various factors, including genetics, age, and health status. Research into equine hemoglobin includes studies on its biochemical properties, the impact of different physiological and pathological conditions on its levels, and its importance in performance and endurance. This page compiles peer-reviewed research studies and scholarly articles that explore the characteristics, regulation, and clinical implications of hemoglobin in equine physiology and health.
Haptoglobin in the serum of thoroughbreds in training. A method is described for the measurement of haptoglobin in equine serum using the peroxidase activity of the haemoglobin-haptoglobin complex. The problems of interference with Fe2+ and Fe3+ ions are described. Normal values for haptoglobin in 629 blood samples from thoroughbreds in training are presented showing a log normal distribution with a 5 per cent to 95 per cent range of 0.42 to 1.7 g/litre. There was no consistent alteration in haptoglobin concentration throughout the season in spite of a change in red cell size and total bilirubin concentration. It is concluded that the measurement ...
Blood-gas, acid-base and haematological values in horses during an endurance ride. The effects of prolonged strenuous exercise on arterial and venous oxygen tension, carbon dioxide tension, pH, bicarbonate, standard bicarbonate, base excess, haemoglobin, packed cell volume and total plasma protein were studied in 36 horses during a 100 km endurance ride. There were significant changes in many parameters when pre-ride values were compared with both mid-ride and end of ride values. The prominent changes were the development of dehydration and a metabolic alkalosis. At the mid-ride sampling time those horses with higher heart rates had a greater degree of metabolic alkalosis th...
Hematological and biochemical values of thoroughbred foals in the first six months of life. Hematological and biochemical parameters in five Thoroughbred foals during the first six months of life are reported. The samples were analyzed for red blood cell, packed cell volume, hemoglobin, platelet, white blood cell, absolute number for leukocytes, and erythrocyte fragility and serum calcium, inorganic phosphorus, sodium, potassium, chloride, magnesium, alkaline phosphatase, icterus index unit, bilirubin, blood urea nitrogen, nonprotein nitrogen, blood glucose, lacticdehydrogenase, glutamic pyruvic transaminase, glutamic oxalacetic transaminase, total protein, albumin, globulin, and A/G...
Hemoglobin polymorphism in Equus przewalskii and E. caballus analyzed by isoelectric focusing. 1. Through the use of isoelectric focusing and peptide analysis, the hemoglobins of Przewalski's horse. Equus przewalskii and the domestic horse, E. caballus have been compared. 2. Przewalski's horses have two separate alpha-globin chain polymorphisms similar to domestic horses. Each hemoglobin phenotype could be accurately determined by isoelectric focusing. 3. Confirmation of the electrofocusing hemoglobin determinations was made by comparison to amino acid composition analyses of purified tryptic peptides and by analysis of the rare hemoglobins phenotypes observed in a family of Norwegian t...
Fourier transform infrared spectroscopic study of molecular interactions in hemoglobin. Infrared absorption spectra of the alpha-104 (G11) cysteine SH group have been observed for aqueous solutions of hemoglobin derivatives from humans, pigs, and horses. The center frequencies ((nu)SH) show ligand sensitive patterns that are similar for the three species, with (nu)SH (HbCO) <(nu)SH (HbO(2) ~ HbCN) < (nu)SH (Hb(+)) <<(nu)SH (deoxyHb) for human and pig hemoglobins. The alpha-104 SH group is most strongly H-bonded (smallest (nu)SH), has the greatest range of (nu)SH (Hb ? HbCO) in human hemoglobin, and is least strongly H-bonded and has the smallest range of (nu)SH (Hb ? HbCO) in hor...
Chronic lead poisoning in horses. Lead acetate was fed to 4 groups of 2 horses each to study chronic lead intoxication. A 5th group of 3 horses was maintained as controls. The leas was fed in capsules, with the minimum dosage of 6.25 mg/kg/day of lead as lead acetate (group I). The dose was increased from group I through group IV in an approximate geometric series, with each group being given about 125% of the dose given the previous group. These doses were given for 105 days, a period designated as phase 1. Since clinical signs were not observed after 105 days, the doses were increased and fed for an additional 190 days (days...
[The interaction between phosphate and protein, and the respiration of the llama, the human fetus and the horse (author’s transl)]. The sequence analysis of llama (Lama glama, Camelidae) hemoglobin is described. The chains were separated, cleaved by trypsin as previously described, quantitatively characterized and sequenced in the sequenator. The llama hemoglobin differs from the human hemoglobin in that it has 25 different amino acids in the alpha chain and 24 different amino acids in the beta chain. The interaction between protein and phosphate is discussed. The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, ...
[Strongyloides westeri Ihle, 1917 (Nematoda: Strongyloididae. II. Parasitological and haematological features of experimental infection (author’s transl)]. Experimental infections using 600,000 infective larvae of Strongyloides westeri were carried out in seven worm-free Shetland ponies, four foals and thee yearlings. In the foals, the prepatent period varied from ten to fourteen days, the patent period ranging from forty-three to eighty-three days. Within approximately two months after infection, a decrease in the concentration of haemoglobin and an increase in the beta-globulin fraction of the protein pattern of the serum, practically coinciding with the maximum S. westeri faecal egg counts, were recorded. In the yearlings, the prepatent period...
[Biochemical and hematological changes in the blood of horses after the “Velká Pardubická” steeple chase]. Blood parameters were studied in two groups of horses in the "Velká Pardubická" steeple-chase in 1974, 1975 and 1976. After the race, the levels of lactate showed a manifold increase; an increase was also ascertained in the levels of glucose, sodium, potassium, haemoglobin, in the haematocrit value and in the number of erythrocytes. The following parameters significantly dropped: the levels of acid-base balance - pH, base excess, bicarbonate levels. It was proved that the values of the same parameters in horses during training were incomparably lower. It is advisable to examine horses thorou...
Studies on a number of erythrocytic enzymes and intermediate products of equine erythrocyte metabolism. The activities and concentrations of a number of erythrocytic enzymes and intermediate products of erythrocyte metabolism were determined in twenty-one normal standard-bred horses which were studied clinically and biochemically. These studies showed that equine anaerobic glycolysis is characterized by a biochemical pattern similar to that observed in human PK deficiency. The greater sensitivity of equine haemoglobin to oxidants is attributable either to low stability of GSH, which may be due either to the low activity of GR or that of 6PGD as observed in the studies. In addition, the saturatio...
Effects of storage on the methaemoglobin content of equine blood. Equine blood containing different levels of methaemoglobin was stored under varying conditions and the methaemoglobin content was monitored during the storage period. Only under aerobic storage at 4 degrees C did the methaemoglobin content of all samples appear to remain stable.
Physiologic responses of the horse to a hot, arid environment. Field investigations were conducted under natural environmental conditions to determine the physiologic responses of rested, hydrated horses (Equus caballus) to the very hot, dry weather characteristic of the summer season in southern Arizona. The emphasis of the investigation was placed on those thermoregulatory mechanisms which are involved in the maintenance of homoiothermy. Rectal temperature of the horses studied remained relatively stable throughout the day, during both cool and hot weather seasons. However, when horses were exposed to hot summer temperatures, rectal temperature (heat st...
Electronic and steric factors affecting ligand binding: horse hemoglobins containing 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme. Horse globin has been recombined with 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme to yield the corresponding reconstituted hemoglobins, and the ligand binding reactions of these reconstituted hemoglobins have been examined in detail. Both hemoglobins exhibit relatively high n values, but 2,4-dimethyldeuterohemoglobin displays a consistently higher oxygen affinity than native hemoglobin, whereas the oxygen affinity of 2,4-dibromodeuterohemoglobin is consistently lower than that of native hemoglobin. The rate constants l’, and 1’4 for the binding of the first and fourth molecules of C...
Training and exercise change respiratory properties of blood in race horses. Effects of training and exercise on blood respiratory properties were investigated in standard-bred race horses. Training caused an increase in the circulating O2 capacity at rest from 18.4 to 21.0 vol%, and in the O2 capacity during exercise from 24.9 to 30.3 vol%. An increase in the in vitro oxygen affinity [P50(PH 7.4, 37.9 degrees C)] of about 2 mm Hg correlated with a decrease in the red cell concentration of 2,3-diphosphoglycerate (DPG) from 6.35 mM-1-1(E), erythrocytes. Trained horses also showed an acute lowering of the red cell DPG concentration after maximal exercise. The physiologic...
Guanidination of horse methemoglobin. Reaction of horse methemoglobin with O-methylisourea at pH 10.2 results in 95% conversion of lysine residues to homoarginine. Analysis of the chymotryptic peptides showed that no single ϵ-amino group was unreactive. Guanidination decreases the dependence of the sedimentation coefficient on hydrogen ion concentration in the range of pH 8 to 11 and did not affect the dependence on protein concentration at pH 7. These results support the conclusion that the lysine side chains involved in subunit contacts have sufficient freedom to accommodate the small changes in bulk and geometry associated wit...
Proton-dependent dissociation equilibrium of hemoglobin. 1. A 700-nanometer light-scattering study on horse methemoglobin in the pH range 4.8 to 7.2. The effect of proton concentration upon the subunit dissociation of horse methemoglobin has been investigated at two ionic strengths by light scattering photometry at 700 nm. Differential refractometry revealed a slight but systematic decrease of the specific refractive index increment with decreasing protein concentration for solutions in dialytic equilibrium with the solvent. In the pH range 4.8-7.2 the dissociation can be described by a simple equilibrium between tetramers and dimers. The dissociation constant Kd of the met derivative is found to be very similar to those of the O2- and CO-l...
Copper and the oxidation of hemoglobin: a comparison of horse and human hemoglobins. Oxidation studies of hemoglobin by Cu(II) indicate that for horse hemoglobin, up to a Cu(II)/heme molar ratio of 0.5, all of the Cu(II) added is used to rapidly oxidize the heme. On the other hand, most of the Cu(II) added to human hemoglobin at low Cu(II)/heme molar ratios is unable to oxidize the heme. Only at Cu(II)/heme molar ratios greater than 0.5 does the amount of oxidation per added Cu(II) approach that of horse hemoglobin. At the same time, binding studies indicate that human hemoglobin has an additional binding site involving one copper for every two hemes, which has a higher copper...
Strongyle infections in ponies. I. Response to intermittent thiabendazole treatments. A group of seven ponies naturally infected with large numbers of small strongyles and raised under conditions to minimize reinfection were treated periodically over a three year span with thiabendazole at the rate of 44 mg/kg body weight. Based on the absence of worm eggs in the feces following each treatment, thiabendazole removed the adult strongyles present with a new population subsequently developing by maturation of inhibited larvae. It took as many as four or five treatments to eliminate or reduce significantly the worm burdens present in the ponies under the conditions of this study. S...
Effects of azaperone on cardiovascular and respiratory functions in the horse. 1 The butyrophenone tranquilizer, azaperone, was administered intramuscularly, at dose levels of 0.4 and 0.8 mg/kg, to ponies and its effects on cardiovascular and respiratory functions assessed. 2 Arterial blood pH, CO2 tension (PaCO2) and O2 tension (PaO2) remained relatively constant throughout the course of action of azaperone. 3 Azaperone did not modify plasma protein concentration but venous blood packed cell volume and haemoglobin concentration were reduced by 5 to 10% for at least 4 hours. These changes were probably caused by uptake of erythrocytes into the splenic reservoir. 4 Small ...
Substrate specificity and modifications of the active centre of elastase-like neutral proteinases from horse blood leucocytes. Two proteinases (2A and 2B) purified from the granular fraction of horse blood leucocytes degrade casein (Km values 12.8 and 6mg/ml respectively) with maximum activity at pH 7.4 and in the presence of 2m-urea. Urea-denatured haemoglobin, fibrinogen, albumin and resorcin/fuchsin-stained elastin are digested at a slower rate. The enzymes hydrolyse synthetic substrates of elastase, N-benzyloxycarbonyl-L-alanine 4-nitrophenyl ester (Km 0.114 and 0.178 mM) and N-acetyl-tri-L-alanine methyl ester (Km 5.55 and 0.98 mM), but they do not hydrolyse synthetic substrates of trypsin, chymotrypsin and throm...