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Author Hedman, J.
Title Heart rate response towards fear-eliciting stimuli in horses Type Manuscript
Year 2003 Publication Sveriges lantbruksuniversitetSveriges lantbruksuniversitet Veterinärprogrammet Abbreviated Journal
Volume (down) 2004 Issue 40 Pages
Keywords horse, fear, heart-rate, novel stimuli
Abstract Finding the right horse for each rider is a difficult task as it is just as important that the temperament of the horse fits the rider as it is that the horse is of the right size. Even though it is a commonly experienced problem, no objective method of easily measuring the horse“s temperament has yet been developed. If it is possible to test horses and get an objective measure of how reactive (emotional) they are, it could be a big help in finding the right horse for each rider. It would be desirable to have a way of testing the horse”s reaction in an unfamiliar (and potentially frightening) situation. In practice this test should be just as easy as it is getting a judgement of its conformation and gaits.

The aim of the present study was to measure individual variation in HR response to different novel objects in horses of the same age, breed and reared in the same environment. We wanted to see whether certain horses (i.e. more emotional horses) react more to novel stimuli, in general, than other horses (i.e. less emotional), irrespective of the type of stimulus. We also wanted to see if different novel stimuli elicited different responses within individuals. The hypothesis was that individuals will react in a similar way to various stimuli.

Twenty four Danish warmblood horses were included in this study. All horses were 2 year-old stallions, reared under similar environmental conditions. They had received a minimum of handling prior to the experimental period. Three different stimuli were used. They were chosen because they were novel to the horses and would elicit measurable fear-reactions in all horses, but not so much that the horses did not approach the feed within the duration of the test. The visual stimulus consisted of a 1meter high orange traffic cone with reflex stripes, placed 1 m in front of the tub, the olfactory stimulus was eucalyptus oil and the auditory stimulus was a radio tuned to white noise. The control was an empty arena.

The result was that only the HR response to the auditory and visual stimuli differed significantly from the control days. The olfactory stimulus did not seem to alarm the horses the way the other stimuli did. We found a tendency towards a correlation in reaction between the olfactory and auditory stimuli and between the auditory and visual stimuli within individuals. These results indicate that horses do not generalize completely in their reaction between different stimuli.
Address
Corporate Author Thesis Bachelor's thesis
Publisher Place of Publication Dept. of Animal Environment and Health, SLU. Examensarbete / Sveriges lantbruksuniversitet, Veterinä Editor
Language Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 1650-7045 ISBN Medium
Area Expedition Conference
Notes Approved no
Call Number Equine Behaviour @ team @ Serial 4652
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Author Rosa, P.A.J.; Azevedo, A.M.; Aires-Barros, M.R.
Title Application of central composite design to the optimisation of aqueous two-phase extraction of human antibodies Type Journal Article
Year 2007 Publication Journal of Chromatography. A Abbreviated Journal J Chromatogr A
Volume (down) 1141 Issue 1 Pages 50-60
Keywords Analysis of Variance; Animals; Antibodies/*chemistry/*isolation & purification; Buffers; Chemical Fractionation/*methods; Horses; Humans; Hydrophobicity; Isoelectric Point; Models, Biological; Molecular Weight; Myoglobin/chemistry/isolation & purification; Osmolar Concentration; Phase Transition; Polyethylene Glycols; Serum Albumin/chemistry/isolation & purification; Sodium Chloride
Abstract The partition of human antibodies in aqueous two-phase systems (ATPSs) of polyethylene glycol (PEG) and phosphate was systematically studied using first pure proteins systems and then an artificial mixture of proteins containing 1mg/ml human immunoglobulin G (IgG), 10mg/ml serum albumin and 2mg/ml myoglobin. Preliminary results obtained using pure proteins systems indicated that the PEG molecular weight and concentration, the pH value and the salts concentration had a pronounced effect on the partitioning behaviour of all proteins. For high ionic strengths and pH values higher than the isoelectric point (pI) of the contaminant proteins, IgG could be selectively recovered on the top phase. According to these results, a face centred composite design was performed in order to optimise the purification of IgG from the mixture of proteins. The optimal conditions for the isolation of IgG were observed for high concentrations of NaCl and low concentrations of both phase forming components. The best purification was achieved using an ATPS containing 8% (w/w) PEG 3350, 10% (w/w) phosphate pH 6 and 15% (w/w) NaCl. A recovery yield of 101+/-7%, a purity of 99+/-0% and a yield of native IgG of 97+/-4% were obtained. Back extraction studies of IgG to a new phosphate phase were performed and higher yields were obtained using 10% phosphate buffer at pH 6. The total extraction yield was 76% and the purity 100%.
Address IBB Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Tecnico, Av Rovisco Pais, 1049-001 Lisbon, Portugal
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0021-9673 ISBN Medium
Area Expedition Conference
Notes PMID:17196214 Approved no
Call Number Serial 1842
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Author Steinhoff, H.J.; Schrader, J.; Schlitter, J.
Title Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals Type Journal Article
Year 1992 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta
Volume (down) 1121 Issue 3 Pages 269-278
Keywords Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry
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.
Address Institut fur Biophysik, Ruhr-Universitat Bochum, Germany
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-3002 ISBN Medium
Area Expedition Conference
Notes PMID:1627604 Approved no
Call Number Equine Behaviour @ team @ Serial 3800
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Author Steinhoff, H.J.; Lieutenant, K.; Redhardt, A.
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
Year 1989 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta
Volume (down) 996 Issue 1-2 Pages 49-56
Keywords Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Hydrogen-Ion Concentration; Methemoglobin/*ultrastructure; Motion; Protein Conformation; Temperature; Thermodynamics; Water
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.
Address Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-3002 ISBN Medium
Area Expedition Conference
Notes PMID:2544230 Approved no
Call Number Equine Behaviour @ team @ Serial 3803
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Author Cho, K.C.; Chan, K.K.
Title Kinetics of cold-induced denaturation of metmyoglobin Type Journal Article
Year 1984 Publication Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology Abbreviated Journal
Volume (down) 786 Issue 1-2 Pages 103-108
Keywords Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart)
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.
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN ISBN Medium
Area Expedition Conference
Notes Approved no
Call Number refbase @ user @ Serial 3978
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Author Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K.
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
Year 1977 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta
Volume (down) 460 Issue 3 Pages 480-489
Keywords Animals; Bacteria; *Cytochrome c Group; *Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics
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.
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-3002 ISBN Medium
Area Expedition Conference
Notes PMID:195599 Approved no
Call Number Equine Behaviour @ team @ Serial 3815
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Author Proudman, C.; Pinchbeck, G.; Clegg, P.; French, N.
Title Equine welfare: risk of horses falling in the Grand National Type Journal Article
Year 2004 Publication Nature Abbreviated Journal Nature
Volume (down) 428 Issue 6981 Pages 385-386
Keywords Accidental Falls/prevention & control/*statistics & numerical data; Animal Welfare; Animals; Great Britain; Horse Diseases/prevention & control; Horses/*physiology; Odds Ratio; Risk Assessment; *Sports
Abstract As in other competitive sports, the famous Grand National steeplechase, which is held at Aintree in the United Kingdom and is watched by 600 million people worldwide, sometimes results in injury. By analysing data from the past 15 Grand National races (consisting of 560 starts by horses), we are able to identify several factors that are significantly associated with failure to complete the race: no previous experience of the course and its unique obstacles, unfavourable ground conditions (too soft or too hard), a large number of runners, and the length of the odds ('starting price'). We also find that there is an increased risk of falling at the first fence and at the jump known as Becher's Brook, which has a ditch on the landing side. Our findings indicate ways in which the Grand National could be made safer for horses and illustrate how epidemiological analysis might contribute to preventing injury in competitive sport.
Address Epidemiology Group, Faculty of Veterinary Science, University of Liverpool, Leahurst, Neston, Wirral CH64 7TE, UK. c.j.proudman@liverpool.ac.uk
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 1476-4687 ISBN Medium
Area Expedition Conference
Notes PMID:15042079 Approved no
Call Number refbase @ user @ Serial 535
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Author Wilson, A.M.; McGuigan, M.P.; Su, A.; van Den Bogert, A.J.
Title Horses damp the spring in their step Type Journal Article
Year 2001 Publication Nature Abbreviated Journal Nature
Volume (down) 414 Issue 6866 Pages 895-899
Keywords Animals; Biomechanics; Elasticity; Forelimb; Gait; Horses/anatomy & histology/*physiology; Leg Bones/*physiology; Locomotion; Models, Biological; Muscle Fibers/physiology; Muscle, Skeletal/anatomy & histology/*physiology; Tendons/anatomy & histology/*physiology; Vibration
Abstract The muscular work of galloping in horses is halved by storing and returning elastic strain energy in spring-like muscle-tendon units.These make the legs act like a child's pogo stick that is tuned to stretch and recoil at 2.5 strides per second. This mechanism is optimized by unique musculoskeletal adaptations: the digital flexor muscles have extremely short fibres and significant passive properties, whereas the tendons are very long and span several joints. Length change occurs by a stretching of the spring-like digital flexor tendons rather than through energetically expensive length changes in the muscle. Despite being apparently redundant for such a mechanism, the muscle fibres in the digital flexors are well developed. Here we show that the mechanical arrangement of the elastic leg permits it to vibrate at a higher frequency of 30-40 Hz that could cause fatigue damage to tendon and bone. Furthermore, we show that the digital flexor muscles have minimal ability to contribute to or regulate significantly the 2.5-Hz cycle of movement, but are ideally arranged to damp these high-frequency oscillations in the limb.
Address Department of Veterinary Basic Sciences, The Royal Veterinary College, Hatfield, Herts AL9 7TA, UK. awilson@rvc.ac.uk
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0028-0836 ISBN Medium
Area Expedition Conference
Notes PMID:11780059 Approved no
Call Number Equine Behaviour @ team @ Serial 2300
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Author Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W.
Title Folding units govern the cytochrome c alkaline transition Type Journal Article
Year 2003 Publication Journal of Molecular Biology Abbreviated Journal J Mol Biol
Volume (down) 331 Issue 1 Pages 37-43
Keywords Animals; Cytochrome c Group/*chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; *Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry
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.
Address Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0022-2836 ISBN Medium
Area Expedition Conference
Notes PMID:12875834 Approved no
Call Number Equine Behaviour @ team @ Serial 3781
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Author Hirota, S.; Suzuki, M.; Watanabe, Y.
Title Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c Type Journal Article
Year 2004 Publication Biochemical and Biophysical Research Communications Abbreviated Journal Biochem Biophys Res Commun
Volume (down) 314 Issue 2 Pages 452-458
Keywords Amino Acids/chemistry; Animals; Cytochromes c/*chemistry; Heme/*chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium/chemistry; Peptides/chemistry; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine/*analogs & derivatives/*chemistry
Abstract Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient absorption spectrum during folding decreased its intensity and red-shifted from 397 to 400 nm by interaction with trityrosine, whereas tyrosinol caused no significant effect. The change in the transient absorption spectrum by interaction with trityrosine was similar to that obtained with 100 mM imidazole, which showed that the population of the intermediate His/His coordinated species increased during folding of cyt c by interaction with trityrosine. The absorption change was biphasic, the fast phase (82+/-9s(-1)) corresponding to the transition from the His/H(2)O to the His/Met coordinated species, whereas the slow phase (24+/-3s(-1)) from His/His to His/Met. By addition of trityrosine, the relative ratio of the slow phase increased, due to increase of the His/His species at the initial stage of folding. According to the resonance Raman spectra of cyt c, the high-spin 6-coordinate and low-spin 6-coordinate species were dominated at pH 2.3 and 4.2, respectively, and these species were not affected by addition of trityrosine. These results demonstrated that the His/His species increased by interaction with trityrosine at the initial stage of cyt c folding, whereas the heme coordination structure was not affected by trityrosine when the protein was completely unfolded or folded. Hydrophobic peptides thus may be useful to study the effects of hydrophobic interactions on protein folding.
Address Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-291X ISBN Medium
Area Expedition Conference
Notes PMID:14733927 Approved no
Call Number Equine Behaviour @ team @ Serial 3777
Permanent link to this record