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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 |
Publication |
The Veterinary Journal |
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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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Author |
Cho, K.C.; Chan, K.K. |
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Title |
Kinetics of cold-induced denaturation of metmyoglobin |
Type |
Journal Article |
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Year |
1984 |
Publication |
Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology |
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Volume |
786 |
Issue |
1-2 |
Pages |
103-108 |
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Keywords |
Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart) |
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Abstract |
Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order. |
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refbase @ user @ |
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3978 |
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Author |
Geutjens, C.A.; Clayton, H.M.; Kaiser, L.J. |
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Title |
Forces and pressures beneath the saddle during mounting from the ground and from a raised mounting platform |
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Journal Article |
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Year |
2008 |
Publication |
The Veterinary Journal |
Abbreviated Journal |
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Volume |
175 |
Issue |
3 |
Pages |
332-337 |
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Keywords |
Electronic saddle mat; Total force; Peak pressure; Equestrian; Kinetics |
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Abstract |
The objective was to use an electronic pressure mat to measure and compare forces and pressures of the saddle on a horse's back when riders mounted from the ground and with the aid of a mounting platform. Ten riders mounted a horse three times each from the ground and from a 35 cm high mounting platform in random order. Total force (summation of forces over all 256 sensors) was measured and compared at specific points on the force-time curve. Total force was usually highest as the rider's right leg was swinging upwards and was correlated with rider mass. When normalized to rider mass, total force and peak pressure were significantly higher when mounting from the ground than from a raised platform (P < 0.05). The area of highest pressure was on the right side of the withers in 97% of mounting efforts, confirming the importance of the withers in stabilizing the saddle during mounting. |
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Admin @ knut @ |
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4344 |
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Author |
Hasumi, H. |
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Title |
Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method |
Type |
Journal Article |
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Year |
1980 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
626 |
Issue |
2 |
Pages |
265-276 |
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Keywords |
Circular Dichroism; *Cytochrome c Group; Hydrogen-Ion Concentration; Isomerism; Kinetics; Spectrophotometry |
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Abstract |
The isomerization of horse-heart ferricytochrome c caused by varying pH was kinetically studied by using circular dichroism (CD) and optical absorption stopped-flow techniques. In the pH range of 7--13, the existence of the three different forms of ferricytochrome c (pH less than 10, pH 10--12, and pH greater than 12) was indicated from the statistical difference CD spectra. On the basis of analyses of the stopped-flow traces in the near-ultraviolet and Soret wavelength regions, the isomerization of ferricytochrome c from neutral form to the above three alkaline forms was interpreted as follows (1) below pH 10, the replacement of the intrinsic ligand of methionine residue by lysine residue occurs; (2) between pH 10 and 12, the uncoupling of the polypeptide chain from close proximity of the heme group occurs first, followed by the interconversion of the intrinsic ligands; and (3) above pH 12, hydroxide form of ferricytochrome c is formed, though the replacement of the intrinsic ligand by extrinsic ligands may occur via different routes from those below pH 12. The CD changes at 288 nm and in the Soret region caused by the pH-jump (down) from pH 6.0 to 1.6 were compared with the appearance of the 620-nm absorption band ascribed to the formation of the high-spin form of ferricytochrome c. Both CD and absorption changes indicated that the isomerization at pH 1.6 consisted of two processes: one proceeded within the dead-time (about 2 ms) of the stopped-flow apparatus and the other proceeded at a determinable rate with the apparatus. On the basis of these results, the isomerization of ferricytochrome c at pH 1.6 was explained as follows: (1) the transition from the low-spin form to the high-spin forms occurs within about 2 ms, the dead-time of the stopped-flow apparatus; and (2) the polypeptide chain is unfolded after the formation of the high-spin form. |
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0006-3002 |
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Notes |
PMID:6260152 |
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no |
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Call Number |
refbase @ user @ |
Serial |
3876 |
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Author |
Alexander, F.; Collett, R.A. |
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Title |
Proceedings: Some observations on the pharmacokinetics of trimethoprim in the horse |
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Journal Article |
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Year |
1974 |
Publication |
British journal of pharmacology |
Abbreviated Journal |
Br J Pharmacol |
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Volume |
52 |
Issue |
1 |
Pages |
142p |
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Keywords |
Animals; Half-Life; Horses/*metabolism; Kinetics; Trimethoprim/*metabolism |
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0007-1188 |
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PMID:4451793 |
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Call Number |
refbase @ user @ |
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112 |
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Author |
Bykov, S.; Lednev, I.; Ianoul, A.; Mikhonin, A.; Munro, C.; Asher, S.A. |
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Title |
Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region |
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Journal Article |
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Year |
2005 |
Publication |
Applied Spectroscopy |
Abbreviated Journal |
Appl Spectrosc |
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Volume |
59 |
Issue |
12 |
Pages |
1541-1552 |
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Keywords |
Animals; Equipment Design; Equipment Failure Analysis; Horses; Kinetics; Metmyoglobin/*analysis; Myocardium/*metabolism; Reproducibility of Results; Sensitivity and Specificity; Spectrophotometry, Ultraviolet/*instrumentation/methods; Spectrum Analysis, Raman/*instrumentation/methods |
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Abstract |
We describe a state-of-the-art tunable ultraviolet (UV) Raman spectrometer for the 193-270 nm spectral region. This instrument allows for steady-state and transient UV Raman measurements. We utilize a 5 kHz Ti-sapphire continuously tunable laser (approximately 20 ns pulse width) between 193 nm and 240 nm for steady-state measurements. For transient Raman measurements we utilize one Coherent Infinity YAG laser to generate nanosecond infrared (IR) pump laser pulses to generate a temperature jump (T-jump) and a second Coherent Infinity YAG laser that is frequency tripled and Raman shifted into the deep UV (204 nm) for transient UV Raman excitation. Numerous other UV excitation frequencies can be utilized for selective excitation of chromophoric groups for transient Raman measurements. We constructed a subtractive dispersion double monochromator to minimize stray light. We utilize a new charge-coupled device (CCD) camera that responds efficiently to UV light, as opposed to the previous CCD and photodiode detectors, which required intensifiers for detecting UV light. For the T-jump measurements we use a second camera to simultaneously acquire the Raman spectra of the water stretching bands (2500-4000 cm(-1)) whose band-shape and frequency report the sample temperature. |
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Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA |
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0003-7028 |
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PMID:16390595 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3767 |
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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 |
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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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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 |
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 |
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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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Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu |
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0022-2836 |
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PMID:12875834 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3781 |
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Author |
Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
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Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
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Journal Article |
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Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
77 |
Issue |
1 |
Pages |
193-199 |
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Keywords |
Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature |
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Abstract |
The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide. |
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0014-2956 |
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PMID:20304 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
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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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English |
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0006-3002 |
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PMID:1627604 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3800 |
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