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Author |
Balendra, G.; Turner, M.; McCrory, P.; Halley, W. |
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Title |
Injuries in amateur horse racing (point to point racing) in Great Britain and Ireland during 1993-2006 |
Type |
Journal Article |
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Year |
2007 |
Publication |
British Journal of Sports Medicine |
Abbreviated Journal |
Br J Sports Med |
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Volume |
41 |
Issue |
3 |
Pages |
162-166 |
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Abstract |
OBJECTIVES: To provide a breakdown of injury incidence from amateur jump racing (also known as point to point racing) in Great Britain and Ireland during 1993-2006 and to compare the injury epidemiology with professional horse racing in Great Britain, Ireland and France. DESIGN: Retrospective review. SETTING: Great Britain and Ireland. PARTICIPANTS: Amateur jockeys. MAIN OUTCOME MEASURES: Injury rates. RESULTS: Injury data suggest that point to point racing is more dangerous from an injury point of view than professional jump racing, which has previously been shown to be more dangerous than flat racing. Amateur jockeys have more falls than their professional counterparts, and this in turn puts them at greater risk of sustaining more serious injuries. CONCLUSIONS: Amateur (point to point) jockeys represent a sporting population that previously has been little studied. They represent a group at high risk of injury, and hence formal injury surveillance tracking and counter measures for injury prevention are recommended. |
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University of Melbourne, Melbourne, Victoria, Australia |
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English |
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1473-0480 |
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PMID:17138629 |
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no |
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Call Number |
refbase @ user @ |
Serial |
3821 |
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Author |
Pinchbeck, G.L.; Clegg, P.D.; Proudman, C.J.; Morgan, K.L.; French, N.P. |
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Title |
Case-control investigation of the factors affecting the risk of horses falling during steeplechase racing in the UK |
Type |
Journal Article |
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Year |
2004 |
Publication |
The Veterinary Record |
Abbreviated Journal |
Vet. Rec. |
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Volume |
155 |
Issue |
1 |
Pages |
11-15 |
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Keywords |
Accidental Falls/*prevention & control/*statistics & numerical data; Animals; Athletic Injuries/epidemiology/etiology/prevention & control/*veterinary; Case-Control Studies; England/epidemiology; Horses/*injuries; Risk Factors; Running/*injuries |
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Abstract |
A concurrent case-control study of 12 UK racecourses was made between March 1, 2000, and August 31, 2001, to identify and quantify the factors associated with the risk of horses falling in steeplechase races. Cases were defined as a jumping effort at a steeplechase fence that resulted in a fall and controls were defined as a successful jumping effort over any steeplechase fence at any of the 12 racecourses within 14 days before or after the case fall. Information on the horse, the jockey and the race were collected and all the fences on all the courses were surveyed. Conditional logistic regression was used to examine the relationships between the predictor variables and the risk of falling. There was one fall per 254 jumping efforts. The risk of a horse falling decreased the more times it had raced on a particular racecourse. The number of fences, the distance from the previous fence and the nature of the previous fence also affected the risk of falling. If the previous fence was a water jump the risk of falling increased; fences that were sited on flat or slight uphill gradients (up to approximately 1 in 25) were associated with a lower risk of horses falling than downhill fences, and higher takeoff boards were associated with a higher risk of falling. |
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Department of Veterinary Clinical Science, University of Liverpool, Leahurst, Neston CH64 7TE |
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ISSN |
0042-4900 |
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Notes |
PMID:15264483 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3773 |
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Author |
Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. |
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Title |
Folding units govern the cytochrome c alkaline transition |
Type |
Journal Article |
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Year |
2003 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
331 |
Issue |
1 |
Pages |
37-43 |
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Keywords |
Animals; Cytochrome c Group/*chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; *Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry |
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Abstract |
The alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways. |
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Address |
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu |
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English |
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ISSN |
0022-2836 |
ISBN |
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Notes |
PMID:12875834 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3781 |
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Author |
Pinchbeck, G.L.; Clegg, P.D.; Proudman, C.J.; Morgan, K.L.; French, N.P. |
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Title |
Case-control study to investigate risk factors for horse falls in hurdle racing in England and Wales |
Type |
Journal Article |
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Year |
2003 |
Publication |
The Veterinary Record |
Abbreviated Journal |
Vet. Rec. |
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Volume |
152 |
Issue |
19 |
Pages |
583-587 |
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Keywords |
Accidental Falls/*statistics & numerical data; Animals; Athletic Injuries/epidemiology/etiology/*veterinary; Case-Control Studies; England/epidemiology; Horses/*injuries; Risk Factors; Running/injuries; Wales/epidemiology |
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Abstract |
Between March 1, 2000 and August 31, 2001, a case-control study was conducted on 12 racecourses in England and Wales to identify and quantify the risk factors associated with horse falls in hurdle races. The cases and controls were defined so that variables relating to the horse, the jockey, the race and racecourse, and the jump could be considered. The cases were defined as a jumping effort at a hurdle flight that resulted in a fall, and the controls were defined as a successful jump over a hurdle at any of the 12 racecourses within 14 days before or after the case fall. Conditional logistic regression was used to examine the univariable and multivariable relationships between the predictor variables and the risk of falling. The risk of falling was significantly associated with the position of the jump in the race, and with the distance and speed of the race. A horse's previous racing experience and history were also significantly associated with the risk of falling and horses participating in their first hurdle race were at almost five times greater risk of falling than horses that had hurdled before. |
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Address |
Epidemiology Group, Department of Veterinary Clinical Science and Animal Husbandry, University of Liverpool, Leahurst, Neston CH64 7TE |
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English |
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Abbreviated Series Title |
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Edition |
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ISSN |
0042-4900 |
ISBN |
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Notes |
PMID:12762486 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3782 |
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Author |
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
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Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
Type |
Journal Article |
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Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
113 |
Issue |
3 |
Pages |
425-433 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism |
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Abstract |
Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion. |
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English |
Summary Language |
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Series Title |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
0014-2956 |
ISBN |
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Notes |
PMID:7011796 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3810 |
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Author |
Jeffcott, L.B.; Dalin, G. |
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Title |
Natural rigaidity of the horse's backbone |
Type |
Journal Article |
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Year |
1980 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
12 |
Issue |
3 |
Pages |
101-108 |
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Keywords |
Animals; Back Pain/physiopathology/veterinary; Horses/*anatomy & histology/physiology; Spine/*anatomy & histology/physiology |
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Abstract |
The functional anatomy of the thoracolumbar (TL) spine is considered in relation to the horse's ability to perform at speed and to jump. The morphological features quite clearly show the relative inflexibility of the equine back and this was confirmed by some experimental studies. Fresh post mortem specimens from 5 Thoroughbreds were used to estimate the limits of dorsoventral movement of the TL spine from mid-thoracic to the cranial lumbar (T10-L2). The individual spinous processes could be moved a mean 1.1-6.0 mm on maximum ventroflexion and 0.8-3.8 mm on dorsiflexion. The overall flexibility of the back was found to be 53.1 mm. Caudal to the mid-point of the back (T13) there was virtually no lateral or rotatory movement of the spine possible. The pathogenesis of some of the common causes of back trouble are discussed including the so-called vertebral subluxation and its treatment by chiropractic manipulation. From an anatomical viewpoint, this condition appears to be a misnomer and may simply be attributable to muscular imbalance leading to aspastic scoliosis. |
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English |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
0425-1644 |
ISBN |
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Notes |
PMID:6447593 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3811 |
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Author |
Czerlinski, G.H.; Erickson, J.O.; Theorell, H. |
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Title |
Chemical relaxation studies on the horse liver alcohol dehydrogenase system |
Type |
Journal Article |
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Year |
1979 |
Publication |
Physiological Chemistry and Physics |
Abbreviated Journal |
Physiol Chem Phys |
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Volume |
11 |
Issue |
6 |
Pages |
537-569 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Buffers; Electron Transport; Ethanol/metabolism; Horses; Hydrogen-Ion Concentration; Liver/*enzymology; Mathematics; NAD/metabolism; Oscillometry; Osmolar Concentration; Temperature; Time Factors |
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Abstract |
Chemical relaxation studies on the system horse liver alcohol dehydrogenase, nicotinamide adenine dinucleotide, and ethanol were conducted observing fluorescence changes between 400 and 500 nm. Temperature-jump experiments were performed at pH 6.5, 7.0, 8.0, and 9.0; concentration-jump experiments at pH 9.0. The reciprocal of the slowest relaxation time was found to be linearly dependent upon the enzyme concentration for relatively low enzyme concentrations, as predicted earlier. Use of the wide pH-range necessitated expression of the four apparent dissociation constants of the catalytic reaction cycle in terms of pH-independent constants. The system was described in terms of only one (or two) catalysis-linked protons not associated with the electron transfer. Protonic steps in a buffered system are in rapid equilibrium, too fast to be measured with the equipment available. Assuming only two of the four bimolecular reaction steps in the four-step cycle are fast compared to the remaining two, six cases may be considered with six expressions for the reciprocal of the slowest relaxation time. Comparison with the experimental data revealed that the bimolecular reaction steps governing the slowest relaxation time change with pH. Above the effective time resolution of the temperature-lump instrument with fluorescence detection (0.1 msec) only one other relaxation time was detectable and only at pH 9. This relaxation time, found to be independent of the concentration of all reactants within experimental error (r = 10 +/- 5 msec), is most likely due to an interconversion among ternary complexes. |
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English |
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Abbreviated Series Title |
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Edition |
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ISSN |
0031-9325 |
ISBN |
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Notes |
PMID:44918 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3813 |
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Author |
Dunn, M.F.; Branlant, G. |
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Title |
Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation |
Type |
Journal Article |
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Year |
1975 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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Volume |
14 |
Issue |
14 |
Pages |
3176-3182 |
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Keywords |
*Alcohol Oxidoreductases/metabolism; Aldehydes/*pharmacology; Animals; Binding Sites; Enzyme Activation/drug effects; Horses; Hydrogen-Ion Concentration; Kinetics; Liver/enzymology; *NAD/analogs & derivatives/pharmacology; Oxidation-Reduction; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; *Zinc/pharmacology |
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Abstract |
1,4,5,6-Tetrahydronicotinamide adenine dinucleotide (H2NADH) has been investigated as a reduced coenzyme analog in the reaction between trans-4-N,N-dimethylaminocinnamaldehyde (I) (lambdamax 398 nm, epsilonmax 3.15 X 10-4 M-minus 1 cm-minus 1) and the horse liver alcohol dehydrogenase-NADH complex. These equilibrium binding and temperature-jump kinetic studies establish the following. (i) Substitution of H2NADH for NADH limits reaction to the reversible formation of a new chromophoric species, lambdamax 468 nm, epsilonmax 5.8 x 10-4 M-minus 1 cm-minus 1. This chromophore is demonstrated to be structurally analogous to the transient intermediate formed during the reaction of I with the enzyme-NADH complex [Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882]. (ii) The process of intermediate formation with the enzyme-NADH complex is independent of pH over the range 6.13-10.54. Although studies were limited to the pH range 5.98-8.72, a similar pH independence appears to hold for the H2NADH system. (iii) Within the ternary complex, I is bound within van der Waal's contact distance of the coenzyme nicotinamide ring. (iv) Formation of the transient intermediate does not involve covalent modification of coenzyme. Based on these findings, we conclude that zinc ion has a Lewis acid function in facilitating the chemical activation of the aldehyde carbonyl for reduction, and that reduced coenzyme plays a noncovalent effector role in this substrate activating step. |
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English |
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ISSN |
0006-2960 |
ISBN |
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Notes |
PMID:238585 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3817 |
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Author |
Czerlinski, G.H.; Wagner, M.; Erickson, J.O.; Theorell, H. |
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Title |
Chemical relaxation studies on the system liver alcohol dehydrogenase, NADH and imidazole |
Type |
Journal Article |
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Year |
1975 |
Publication |
Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry |
Abbreviated Journal |
Acta Chem Scand B |
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Volume |
29 |
Issue |
8 |
Pages |
797-810 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Computers; Hydrogen-Ion Concentration; Imidazoles/*metabolism; Kinetics; Liver/enzymology/*metabolism; Mathematics; Models, Chemical; NAD/*metabolism; Time Factors |
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Abstract |
Several years ago, Theorell and Czerlinski conducted experiments on the system of horse liver alcohol dehydrogenase, reduced nicotinamide adenine dinucleotide and imidazole, using the first version of the temperature jump apparatus with detection of changes in fluorescence. These early experiments were repeated with improved instrumentation and confirmed the early experiments in general terms. However, the improved detection system allowed to measure a slight concentration dependence of the relaxation time of around 3 ms. Furthermore, the chemical relaxation time was smaller than the one determined earlier (by factor 2). The data were evaluated much more rigorously than before, allowing an appropriate interpretation of the results. The observed relaxation time is largely due to rate constants in an interconversion of ternary complexes, which are faster than three (of the four) dissociation rate constants, determined previously by Theorell and McKinley-McKee.1,2 This fact contributed to earlier difficulties of finding any concentration dependence. However, the binding of imidazole to the binary enzyme-coenzyme complex can be made to couple kinetically into the interconversion rate of the two ternary complexes. The observed signal derives largely from the ternary complex(es). A substantial fluorescence signal change is associated with the observed relaxation process, suggesting a relocation of the imidazole in reference to the nicotinamide moiety of the bound coenzyme. Nine models are considered with two types of coupling of pre-equilibria (none-all). Quantitative evaluations favor the model with two ternary complexes connected by an interconversion outside the four-step (bimolecular) cycle. The ternary complex outside the cycle has much higher fluorescence yield than the one inside. The interconversion equilibrium is near unity for imidazole. If it would be shifted very much to the side of the “dead-end” complex (as in isobutyramide?!), stimulating action could not take place. |
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English |
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ISSN |
0302-4369 |
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Notes |
PMID:882 |
Approved |
no |
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Call Number |
refbase @ user @ |
Serial |
3887 |
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Author |
Huizinga, H.A.; van der Werf, J.H.J.; Korver, S.; van der Meij, G.J.W. |
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Title |
Stationary performance testing of stallions from the Dutch Warmblood riding horse population. 1. Estimated genetic parameters of scored traits and the genetic relation with dressage and jumping competition from offspring of breeding stallions |
Type |
Journal Article |
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Year |
1991 |
Publication |
Livestock Production Science |
Abbreviated Journal |
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Volume |
27 |
Issue |
2-3 |
Pages |
231-244 |
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Keywords |
dressage; genetic parameters; horse; jumping; performance; stallion |
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Abstract |
The stationary performance testing (SPT) of stallions as breeding candidates in the Dutch Warmblood riding horse population is evaluated. Genetic and phenotypic parameters of traits scored during SPT and the genetic correlation of these traits with performances in dressage and jumping competition from offspring of breeding stallions are estimated. Data from 1978-1988 are used, covering scores from 337 3-year-old stallions. Eight subjectively scored traits are considered. These traits are: walk; trot; canter; riding ability; show jumping; free jumping; cross country; character. SPT lasts for a period of 100 days. Data from SPT are analysed using an animal model. The relations between SPT of stallions and performances in jumping and dressage competition are analysed with an animal model for SPT data and a sire model for competition data. Variance and covariance components are estimated by restricted maximum likelihood (REML) procedures. Estimates of heritability are high (0.64) for gaits and riding ability, intermediate (0.41) for cross country and medium-high (0.31) for jumping. Estimated genetic correlation between show jumping scored during SPT and jumping in competition from offspring of breeding stallions is 0.84; for dressage this relation is 0.83. Some possible bias due to selection and the subjectivity of scoring is discussed. It is indicated that selection on SPT of stallions before entering breeding service is an effective tool to breed for ability of performance in competition. |
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Call Number |
refbase @ user @ |
Serial |
3962 |
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