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Author |
Steinhoff, H.J.; Schrader, J.; Schlitter, J. |
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Title |
Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals |
Type |
Journal Article |
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Year |
1992 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal  |
Biochim Biophys Acta |
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Volume |
1121 |
Issue |
3 |
Pages |
269-278 |
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Keywords |
Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry |
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Abstract |
Association equilibria and association kinetics of the thiocyanate binding reaction to methemoglobin in single crystals and solution are studied using temperature-jump technique and polarized absorption spectroscopy. Different kinetic constants are found for the reaction in solution and crystal phase for the alpha- and beta-subunits of the methemoglobin tetramer. The reduction of the reactivity of the alpha- and beta-subunits in crystalline phase is 6-fold and 2.4-fold, respectively, compared to the values found in solution. The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals. Our results suggest that crystallization of hemoglobin has little influence on small-scale structural fluctuations which are necessary for ligands to get to the binding sites and large-scale structural motions are suppressed. |
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Institut fur Biophysik, Ruhr-Universitat Bochum, Germany |
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0006-3002 |
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PMID:1627604 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3800 |
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Author |
Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. |
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Title |
Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements |
Type |
Journal Article |
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Year |
1989 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
996 |
Issue |
1-2 |
Pages |
49-56 |
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Keywords |
Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Hydrogen-Ion Concentration; Methemoglobin/*ultrastructure; Motion; Protein Conformation; Temperature; Thermodynamics; Water |
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Abstract |
Temperature-dependent EPR and temperature-jump measurements have been carried out, in order to examine the high-spin to low-spin transition of aquomethemogobin (pH 6.0). Relaxation rates and equilibrium constants could be determined as a function of temperature. As a reaction mechanism for the high-spin to low-spin transition, the binding of N epsilon of His E7 to the heme iron had been proposed; the same mechanism had been suggested for the ms-effect, found in temperature-jump experiments on aquomethemoglobin. A comparison of the thermodynamic quantities, deduced form the measurements in this paper, gives evidence that indeed the same reaction is investigated in both cases. Our results and most of the findings of earlier studies on the spin-state transitions of aquomethemoglobin, using susceptibility, optical, or EPR measurements, can be explained by the transition of methemoglobin with H2O as ligand (with high-spin state at all temperatures) and methemoglobin with ligand N epsilon of His E7 (with a low-spin ground state). Thermal fluctuations of large amplitude have to be postulated for the reaction to take place, so this reaction may be understood as a probe for the study of protein dynamics. |
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Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G |
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0006-3002 |
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PMID:2544230 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3803 |
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Author |
Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K. |
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Title |
Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide |
Type |
Journal Article |
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Year |
1977 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
460 |
Issue |
3 |
Pages |
480-489 |
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Keywords |
Animals; Bacteria; *Cytochrome c Group; *Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics |
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Abstract |
The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. (Formula: see text.) Thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. The results of this showed that (1) the redox potential of cytochrome c-552, + 0.19 V, is markedly less than that of horse heart cytochrome c. (2) deltaHox of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) deltaSox and deltaSred of cytochrome c-552 are more negative than those of horse heart cytochrome c. (4) kred of cytochrome c-552 is much lower than that of horse heart cytochrome c at room temperature. |
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0006-3002 |
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Notes |
PMID:195599 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3815 |
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Author |
Kirkpatrick, J.F.; Vail, R.; Devous, S.; Schwend, S.; Baker, C.B.; Wiesner, L. |
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Title |
Diurnal variation of plasma testosterone in wild stallions |
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Journal Article |
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Year |
1976 |
Publication |
Biology of reproduction |
Abbreviated Journal |
Biol Reprod |
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Volume |
15 |
Issue |
1 |
Pages |
98-101 |
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Keywords |
Animals; *Circadian Rhythm; Horses/*blood; Male; Montana; Sexual Behavior, Animal; Species Specificity; Testosterone/*blood |
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0006-3363 |
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Notes |
PMID:986195 |
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Call Number |
refbase @ user @ |
Serial |
149 |
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Author |
Morton, D.B. |
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Title |
Self-consciousness and animal suffering |
Type |
Journal Article |
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Year |
2000 |
Publication |
Biologist (London, England) |
Abbreviated Journal |
Biologist (London) |
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Volume |
47 |
Issue |
2 |
Pages |
77-80 |
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Keywords |
Animal Population Groups/*psychology; Animal Welfare/*standards; Animals; Behavior, Animal; *Consciousness; Dogs; *Ego; Horses/psychology; Pain/psychology/*veterinary; Pan troglodytes/psychology; Parrots; Pongo pygmaeus/psychology; Self Concept |
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Abstract |
Animals with relatively highly developed brains are likely to experience some degree of self-awareness and the ability to think. As well as being interesting in its own right, self-consciousness matters from an ethical point of view, since it can give rise to forms of suffering above and beyond the immediate physical sensations of pain or distress. This article surveys the evidence for animal self-consciousness and its implications for animal welfare. |
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Address |
Division of Primary Care, Public and Occupational Health, School of Medicine, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. d.b.morton@bham.ac.uk |
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0006-3347 |
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PMID:11190233 |
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Call Number |
refbase @ user @ |
Serial |
618 |
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Author |
Gulotta, M.; Rogatsky, E.; Callender, R.H.; Dyer, R.B. |
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Title |
Primary folding dynamics of sperm whale apomyoglobin: core formation |
Type |
Journal Article |
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Year |
2003 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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Volume |
84 |
Issue |
3 |
Pages |
1909-1918 |
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Keywords |
Animals; Apoproteins/*chemistry; Crystallography/*methods; Horses; Myocardium/chemistry; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Species Specificity; Structure-Activity Relationship; Temperature; Whales |
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Abstract |
The structure, thermodynamics, and kinetics of heat-induced unfolding of sperm whale apomyoglobin core formation have been studied. The most rudimentary core is formed at pH(*) 3.0 and up to 60 mM NaCl. Steady state for ultraviolet circular dichroism and fluorescence melting studies indicate that the core in this acid-destabilized state consists of a heterogeneous composition of structures of approximately 26 residues, two-thirds of the number involved for horse heart apomyoglobin under these conditions. Fluorescence temperature-jump relaxation studies show that there is only one process involved in Trp burial. This occurs in 20 micro s for a 7 degrees jump to 52 degrees C, which is close to the limits placed by diffusion on folding reactions. However, infrared temperature jump studies monitoring native helix burial are biexponential with times of 5 micro s and 56 micro s for a similar temperature jump. Both fluorescence and infrared fast phases are energetically favorable but the slow infrared absorbance phase is highly temperature-dependent, indicating a substantial enthalpic barrier for this process. The kinetics are best understood by a multiple-pathway kinetics model. The rapid phases likely represent direct burial of one or both of the Trp residues and parts of the G- and H-helices. We attribute the slow phase to burial and subsequent rearrangement of a misformed core or to a collapse having a high energy barrier wherein both Trps are solvent-exposed. |
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Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA. gulotta@aecom.yu.edu |
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0006-3495 |
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Notes |
PMID:12609893 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3783 |
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Author |
Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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Title |
Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump |
Type |
Journal Article |
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Year |
2000 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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Volume |
78 |
Issue |
1 |
Pages |
405-415 |
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Keywords |
Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence |
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Abstract |
Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation. |
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Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia |
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ISSN |
0006-3495 |
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Notes |
PMID:10620304 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3792 |
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Author |
Gonzalez-Fernandez, J.M.; Atta, S.E. |
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Title |
Facilitated transport of oxygen in the presence of membranes in the diffusion path |
Type |
Journal Article |
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Year |
1982 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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Volume |
38 |
Issue |
2 |
Pages |
133-141 |
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Keywords |
Animals; Biological Transport, Active; Cell Membrane/*metabolism; Diffusion; Dogs; Horses; Humans; Kinetics; Mathematics; *Models, Biological; Muscles/*metabolism; Oxygen/*metabolism |
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Abstract |
Most of the experimental observations on facilitated transport have been done with millipore filters, and all the theoretical studies have assumed homogeneous spatial properties. In striated muscle there exist membranes that may impede the diffusion of the carrier myoglobin. In this paper a theoretical study is undertaken to analyze the transport in the presence of membranes in the diffusion path. For the numerical computations physiologically relevant values of the parameters were chosen. The numerical results indicate that the presence of membranes tends to decrease the facilitation. For the nonlinear chemical kinetics of the reaction of oxygen with the carrier, this decrement also depends on the location of the membranes. At the higher oxygen concentration side of each membrane the flow of combined oxygen is transferred to the flow of dissolved oxygen. The reverse process occurs at the lower concentration side. Jump discontinuities of the concentration of the oxygen-carrier compound at each membrane are associated with these transfers. The decrement of facilitation is due to the cumulative effect of these jump discontinuities. |
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0006-3495 |
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PMID:7093418 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3806 |
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Author |
Cancedda, M. |
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Title |
[Social and behavioral organization of horses on the Giara (Sardinia): distribution and aggregation] |
Type |
Journal Article |
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Year |
1990 |
Publication |
Bollettino della Societa italiana di biologia sperimentale |
Abbreviated Journal |
Boll Soc Ital Biol Sper |
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Volume |
66 |
Issue |
11 |
Pages |
1089-1096 |
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Keywords |
Animals; *Animals, Wild/physiology/psychology; Environment; Female; *Horses/physiology/psychology; Italy; Male; Population Density; Sexual Behavior, Animal; *Social Behavior; Social Dominance; Water |
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In this paper some considerations on the environment of the 42 Kmq of the volcanic-basaltic Giara tableland are discussed. Conditioning by the environment and its effect on the distribution of a population of 712 horses is illustrated in view of their social and behavioural organization. |
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Istituto di Fisiologia Generale e Speciale, Universita di Sassari |
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Italian |
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Introduzione all'organizzazione sociale e comportamentale dei cavallini sulla Giara (Sardegna): distribuzione ed aggregazione |
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0037-8771 |
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PMID:2095819 |
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no |
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Call Number |
refbase @ user @ |
Serial |
673 |
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Author |
Verheyen, K.; Price, J.; Lanyon, L.; Wood, J. |
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Title |
Exercise distance and speed affect the risk of fracture in racehorses |
Type |
Journal Article |
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Year |
2006 |
Publication |
Bone |
Abbreviated Journal |
Bone |
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Volume |
39 |
Issue |
6 |
Pages |
1322-1330 |
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Keywords |
Animals; Case-Control Studies; Cohort Studies; England; Exertion; Female; Fractures, Bone/etiology/*veterinary; Horse Diseases/*etiology; Horses/*injuries; Male; Physical Conditioning, Animal/adverse effects/methods; Poisson Distribution; Prospective Studies; Regression Analysis; Risk Factors; Running/injuries/physiology |
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Abstract |
In order to gain insight into those training regimens that can minimise the risk of fracture in athletic populations, we conducted a large epidemiological study in racehorses. Thoroughbred racehorses provide a suitable model for studying fracture development and exercise-related risk factors in physically active populations. They represent a homogeneous population, undertaking intensive exercise programmes that are sufficiently heterogeneous to determine those factors that influence injury risk. Daily exercise information was recorded for a cohort of 1178 thoroughbreds that were monitored for up to 2 years. A total of 148 exercise-induced fractures occurred in the study population. Results from a nested case-control study showed a strong interactive effect of exercise distances at different speeds on fracture risk. Horses that exceeded 44 km at canter (< or =14 m/s) and 6 km at gallop (>14 m/s) in a 30-day period were at particularly increased risk of fracture. These distances equate to ca. 7700 bone loading cycles at canter and 880 loading cycles at gallop. Fifty-six fractures occurred in the subset of study horses that were followed since entering training as yearlings, when skeletally immature (n = 335). Cohort analysis of this data set showed that, in previously untrained bones, accumulation of canter exercise increased the risk of fracture (P < or = 0.01), whereas accumulation of high-speed gallop exercise had a protective effect (P < 0.01). However, increasing distances at canter and gallop in short time periods (up to one month) were associated with an increasing fracture risk. All training exercise involves a balance between the risk of fracture inherent in exposure to loading and the beneficial effect that loading has by stimulating bone cells to produce a more robust architecture. Results from our study provide important epidemiological evidence of the effects of physical exercise on bone adaptation and injury risk and can be used to inform the design of safer exercise regimens in physically active populations. |
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Epidemiology Unit, Animal Health Trust, Newmarket, United Kingdom. kverheyen@rvc.ac.uk |
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English |
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8756-3282 |
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Notes |
PMID:16926125 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4030 |
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