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Meschan, E.M.; Peham, C.; Schobesberger, H.; Licka, T.F. |
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Title |
The influence of the width of the saddle tree on the forces and the pressure distribution under the saddle |
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Journal Article |
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Year |
2007 |
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The Veterinary Journal |
Abbreviated Journal |
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Volume |
173 |
Issue  |
3 |
Pages |
578-584 |
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Keywords |
Saddle fit; Kinematics; Kinetics; Pressure; Saddletree |
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Abstract |
As there is no statistical evidence that saddle fit influences the load exerted on a horse's back this study was performed to assess the hypothesis that the width of the tree significantly alters the pressure distribution on the back beneath the saddle. Nineteen sound horses were ridden at walk and trot on a treadmill with three saddles differing only in tree width. Kinetic data were recorded by a sensor mat. A minimum of 14 motion cycles were used in each trial. The saddles were classified into four groups depending on fit. For each horse, the saddle with the lowest overall force (LOF) was determined. Saddles were classified as “too-narrow” if they were one size (2 cm) narrower than the LOF saddle, and “too-wide” if they were one size (2 cm) wider than the LOF saddle. Saddles two sizes wider than LOF saddles were classified as “very-wide”. In the group of narrow saddles, the pressure in the caudal third (walk 0.63 N/cm2 +/- 0.10; trot 1.08 N/cm2 +/- 0.26) was significantly higher compared to the LOF saddles (walk 0.50 N/cm2 +/- 0.09; trot 0.86 N/cm2 +/- 0.28). In the middle transversal third, the pressure of the wide saddles (walk 0.73 N/cm2 +/- 0.06; trot 1.52 N/cm2 +/- 0.19) and very-wide saddles (walk 0.77 N/cm2 +/- 0.06; trot 1.57 N/cm2 +/- 0.19) was significantly higher compared to LOF saddles (walk 0.65 N/cm2 +/- 0.10/ 0.63 N/cm2 +/- 0.11; trot 1.33 N/cm2 +/- 0.22/1.27 N/cm2 +/- 0.20). This study demonstrates that the load under poorly fitting saddles is distributed over a smaller area than under properly fitting saddles, leading to potentially harmful pressures peaks. |
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Admin @ knut @ |
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4349 |
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Jallon, J.M.; Risler, Y.; Iwatsubo, M. |
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Title |
Beef liver L-Glutamate dehydrogenase mechanism: presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH |
Type |
Journal Article |
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Year |
1975 |
Publication |
Biochemical and biophysical research communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
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Volume |
67 |
Issue |
4 |
Pages |
1527-1536 |
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Keywords |
Animals; Cattle; Glutamate Dehydrogenase/*metabolism; Ketoglutaric Acids; Kinetics; Liver/*enzymology; Nadp; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet |
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0006-291X |
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PMID:1038 |
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Admin @ knut @ |
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21 |
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Author |
Hagen, S.J.; Eaton, W.A. |
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Title |
Two-state expansion and collapse of a polypeptide |
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Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
301 |
Issue |
4 |
Pages |
1019-1027 |
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Keywords |
Animals; Computer Simulation; Cytochrome c Group/*chemistry/*metabolism; Horses; Kinetics; Lasers; Models, Chemical; Peptides/*chemistry/*metabolism; Protein Conformation; Protein Denaturation; *Protein Folding; Spectrometry, Fluorescence; Temperature; Thermodynamics |
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Abstract |
The initial phase of folding for many proteins is presumed to be the collapse of the polypeptide chain from expanded to compact, but still denatured, conformations. Theory and simulations suggest that this collapse may be a two-state transition, characterized by barrier-crossing kinetics, while the collapse of homopolymers is continuous and multi-phasic. We have used a laser temperature-jump with fluorescence spectroscopy to measure the complete time-course of the collapse of denatured cytochrome c with nanosecond time resolution. We find the process to be exponential in time and thermally activated, with an apparent activation energy approximately 9 k(B)T (after correction for solvent viscosity). These results indicate that polypeptide collapse is kinetically a two-state transition. Because of the observed free energy barrier, the time scale of polypeptide collapse is dramatically slower than is predicted by Langevin models for homopolymer collapse. |
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Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Building 5, Bethesda, MD, 20892-0520, USA |
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0022-2836 |
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PMID:10966803 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3790 |
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Author |
Dyson, H.J.; Beattie, J.K. |
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Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
Type |
Journal Article |
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Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
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Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
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Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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0021-9258 |
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PMID:6277891 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Pierce, M.M.; Nall, B.T. |
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Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
Type |
Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
298 |
Issue |
5 |
Pages |
955-969 |
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Keywords |
Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/*chemistry/genetics/*metabolism; *Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/*metabolism; Histidine/genetics/*metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/*chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics |
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Abstract |
The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand. |
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Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA |
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0022-2836 |
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PMID:10801361 |
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no |
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Call Number |
refbase @ user @ |
Serial |
3853 |
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Author |
Saigo, S. |
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Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
Type |
Journal Article |
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Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
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Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
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Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
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Abstract |
Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH. |
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0021-924X |
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PMID:6270075 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. |
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Title |
Nature of the fast and slow refolding reactions of iron(III) cytochrome c |
Type |
Journal Article |
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Year |
1981 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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Volume |
20 |
Issue |
6 |
Pages |
1622-1630 |
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Keywords |
Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis |
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Abstract |
The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding. |
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0006-2960 |
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PMID:6261802 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3809 |
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Author |
Ryan, C.T.; Schaer, B.L.D.; Nunamaker, D.M. |
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Title |
A novel wireless data acquisition system for the measurement of hoof accelerations in the exercising horse |
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Journal Article |
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Year |
2006 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
38 |
Issue |
7 |
Pages |
671-674 |
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Keywords |
*Acceleration; Animals; Biomechanics; Equipment and Supplies/*veterinary; Hoof and Claw/*physiology; Horses/*physiology; Kinetics; Musculoskeletal Physiology; Physical Conditioning, Animal/*physiology; Running/physiology |
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Abstract |
REASONS FOR PERFORMING STUDY: A device is needed to safely and wirelessly evaluate accelerations experienced by the horse hoof under a variety of surface conditions with the horse exercising at training or racing speeds. OBJECTIVES: To develop a miniaturised wireless data acquisition system (WDAS) which reliably records hoof accelerations and the times over which they occur in a minimally invasive manner in the exercising Thoroughbred. METHODS: The following criteria were set for device development: production of a lightweight and minimally invasive system, which provides an adequate acceleration range, appropriate frequency response to capture high speed events, and compatibility with a low power wireless telemetry system. Following device development, the WDAS was calibrated, and tested in 6 Thoroughbred horses over a variety of surfaces. RESULTS: Collection of acceleration in seven trials using 6 horses over a variety of surfaces resulted in repeatable acceleration data with respect to the overall characteristic shape of the impact profile. Impact accelerations varied with surface, ranging 34.8-191.7 g. Accelerations on take off were in a similar range, although higher in some trials. Peak impact accelerations tended to larger over the grass paddock surface, than either the indoor arena or the dirt track. During dirt track trials, accelerations on take-off were often comparably larger than those observed on impact within the same footfall. CONCLUSIONS: This study reports the development of a wireless system that successfully measures hoof acceleration in a minimally invasive manner over a variety of surface and exercise conditions. POTENTIAL RELEVANCE: The WDAS will be used in further studies to evaluate various components of the horse-racetrack interface, in an attempt to identify risk factors for musculoskeletal injury in the Thoroughbred racehorse. |
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Richard S. Reynolds, Jr. Comparative Orthopedic Research Laboratory, Department of Clinical Studies, New Bolton Center, School of Veterinary Medicine, University of Pennsylvania, Kennett Square, Pennsylvania 19348, USA |
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0425-1644 |
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PMID:17228584 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4023 |
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Author |
Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. |
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Title |
Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c |
Type |
Journal Article |
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Year |
2004 |
Publication |
The Protein Journal |
Abbreviated Journal |
Protein J |
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Volume |
23 |
Issue |
8 |
Pages |
519-527 |
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Keywords |
Animals; Cytochromes c/*chemistry; Enzyme Activation; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry |
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Abstract |
We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal. |
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Address |
Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 7/A 43100 Parma, Italy |
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1572-3887 |
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PMID:15648974 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3770 |
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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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Series Editor |
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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 |
0302-4369 |
ISBN |
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Medium |
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Area |
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Expedition |
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Conference |
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Notes |
PMID:882 |
Approved |
no |
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Call Number |
refbase @ user @ |
Serial |
3887 |
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| Permanent link to this record |
