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Dyson, H.J.; Beattie, J.K. |
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Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
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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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Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Tsong, T.Y. |
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Title |
Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
Type |
Journal Article |
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Year |
1977 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
252 |
Issue |
24 |
Pages |
8778-8780 |
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Keywords |
*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
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Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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PMID:200618 |
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refbase @ user @ |
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3882 |
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Author |
de Waal, F.B. |
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Title |
Macaque social culture: development and perpetuation of affiliative networks |
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Journal Article |
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Year |
1996 |
Publication |
Journal of comparative psychology (Washington, D.C. : 1983) |
Abbreviated Journal |
J Comp Psychol |
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Volume |
110 |
Issue |
2 |
Pages |
147-154 |
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Keywords |
Animals; Dominance-Subordination; Female; Macaca mulatta/*psychology; Male; Maternal Behavior; *Peer Group; Sexual Behavior, Animal; *Social Behavior; Social Distance; *Social Environment |
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Maternal affiliative relations may be transmitted to offspring, similar to the way in which maternal rank determines offspring rank. The development of 23 captive female rhesus monkeys (Macaca mulatta) was followed from the day of birth until adulthood. A multivariate analysis compared relations among age peers with affiliative relations, kinship, and rank distance among mothers. Maternal relations were an excellent predictor of affiliative relations among daughters, explaining up to 64% of the variance. Much of this predictability was due to the effect of kinship. However, after this variable had been controlled, significant predictability persisted. For relations of female subjects with male peers, on the other hand, maternal relations had no significant predictive value beyond the effect of kinship. One possible explanation of these results is that young rhesus females copy maternal social preferences through a process of cultural learning. |
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Department of Psychology, Emory University, Atlanta, Georgia 30322, USA. dewaal@rmy.emory.edu |
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0735-7036 |
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PMID:8681528 |
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no |
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Call Number |
refbase @ user @ |
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204 |
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Author |
Wasserman, E.A. |
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Title |
The science of animal cognition: past, present, and future |
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Journal Article |
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Year |
1997 |
Publication |
Journal of Experimental Psychology. Animal Behavior Processes |
Abbreviated Journal |
J Exp Psychol Anim Behav Process |
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Volume |
23 |
Issue |
2 |
Pages |
123-135 |
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Keywords |
Animal Communication; Animal Population Groups/*psychology; Animals; Behavior, Animal; Behavioral Sciences/*trends; *Cognition; Evolution; Forecasting; Humans; Intelligence |
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The field of animal cognition is strongly rooted in the philosophy of mind and in the theory of evolution. Despite these strong roots, work during the most famous and active period in the history of our science-the 1930s, 1940s, and 1950s-may have diverted us from the very questions that were of greatest initial interest to the comparative analysis of learning and behavior. Subsequently, the field has been in steady decline despite its increasing breadth and sophistication. Renewal of the field of animal cognition may require a return to the original questions of animal communication and intelligence using the most advanced tools of modern psychological science. Reclaiming center stage in contemporary psychology will be difficult; planning that effort with a host of strategies should enhance the chances of success. |
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Department of Psychology, University of Iowa, Iowa City 52242-1407, USA. ed-wasserman@uiowa.edu |
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0097-7403 |
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Notes |
PMID:9095537 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2779 |
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Author |
Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M. |
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Title |
Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) |
Type |
Journal Article |
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Year |
1979 |
Publication |
Journal of Inorganic Biochemistry |
Abbreviated Journal |
J Inorg Biochem |
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Volume |
11 |
Issue |
2 |
Pages |
95-100 |
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Keywords |
Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism |
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Abstract |
The electron transfer reactions between Rhus vernicifera stellacyanin and either horse heart cytochrome c or Pseudomonas aeruginosa cytochrome c551 were investigated by rapid reaction techniques. The time course of electron transfer is monophasic under all conditions, and thus consistent with a simple formulation of the reaction. Both stopped-flow and temperature-jump experiments yield equilibrium constants in reasonable agreement with values calculated from the redox potentials. The differences in reaction rate between the two cytochromes and stellacyanin are discussed in terms of the Marcus theory. |
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0162-0134 |
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PMID:228006 |
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Call Number |
refbase @ user @ |
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3879 |
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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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Call Number |
Equine Behaviour @ team @ |
Serial |
3781 |
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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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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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no |
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Call Number |
Equine Behaviour @ team @ |
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3790 |
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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 |
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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 |
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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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 |
Curtis, S.E.; Stricklin, W.R. |
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The importance of animal cognition in agricultural animal production systems: an overview |
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Journal Article |
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Year |
1991 |
Publication |
Journal of Animal Science |
Abbreviated Journal |
J. Anim Sci. |
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69 |
Issue |
12 |
Pages |
5001-5007 |
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*Agriculture; Animal Population Groups/*psychology; *Animal Welfare; Animals; *Behavior, Animal; *Cognition; Heat; Helplessness, Learned; Housing, Animal/standards; Immobilization; Nesting Behavior; Pain/psychology/veterinary |
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To describe and then fulfill agricultural animals' needs, we must learn more about their fundamental psychological and behavioral processes. How does this animal feel? Is that animal suffering? Will we ever be able to know these things? Scientists specializing in animal cognition say that there are numerous problems but that they can be overcome. Recognition by scientists of the notion of animal awareness has been increasing in recent years, because of the work of Griffin and others. Feeling, thinking, remembering, and imagining are cognitive processes that are factors in the economic and humane production of agricultural animals. It has been observed that the animal welfare debate depends on two controversial questions: Do animals have subjective feelings? If they do, can we find indicators that reveal them? Here, indirect behavioral analysis approaches must be taken. Moreover, the linear additivity of several stressor effects on a variety of animal traits suggests that some single phenomenon is acting as a “clearinghouse” for many or all of the stresses acting on an animal at any given time, and this phenomenon might be psychological stress. Specific situations animals may encounter in agricultural production settings are discussed with respect to the animals' subjective feelings. |
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University of Illinois, Urbana 61801 |
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0021-8812 |
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PMID:1808193 |
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Equine Behaviour @ team @ |
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2754 |
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Author |
Suagee-Bedore, J.K.; Linden, D.R.; Bennett-Wimbush, K. |
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Title |
Effect of Pen Size on Stress Responses of Stall-Housed Horses Receiving One Hour of Daily Turnout |
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Journal Article |
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Year |
2021 |
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Journal of Equine Veterinary Science |
Abbreviated Journal |
J. Equine Vet. Sci. |
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98 |
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103366 |
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Agonistic behaviors; Cortisol; Group turnout; Paddock sizes |
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Group turnout provides important socializing opportunities for horses, particularly those that are primarily stalled. A high percentage of equine injuries occur during group turnout, which could partly be due to the physical constraints of fencing. To investigate appropriate paddock sizes for group turnouts, horses (n = 12) from a single herd were divided into groups of 4, stalled for 24 hours, and then turned out for 1 hour into one of three differently sized pens: 342, 263, and 184 m2 per horse. Groups rotated through pens across 3 days, receiving one treatment per day. Blood was sampled for cortisol concentrations at 08:00 hours each morning, and then at 15 and 60 minutes into the turn out sessions, and 60 minutes after return to individual stalls. Groups rotated through three turnout times: 09:00, 12:00, 14:00 hours. Counts of agonistic behaviors (chasing, contact biting, and kicking) and low-level threats (pinned ears, tail swishing, bite and kick threats) were recorded. When turned out in pens that provided 342 m2 per horse, horses exhibited reduced plasma cortisol concentrations by 15 minutes after turnout and at 1 hour after return to their stalls (P < .05). Horses in pens providing 184 m2 per horse exhibited greater agonistic (P < .001) and low-level threat (P < .01) behaviors than horses in larger pens. These data provide insight into appropriate pen sizes for horses from established herds. Providing at least 342 m2 per horse may reduce the chance of injury in horses accustomed to group turnout. |
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0737-0806 |
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Equine Behaviour @ team @ |
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6694 |
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