| Records |
| Author |
McDonnell, S.M.; Poulin, A. |
| Title |
Equid play ethogram |
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Journal Article |
| Year |
2002 |
Publication |
Applied Animal Behaviour Science |
Abbreviated Journal |
Appl. Anim. Behav. Sci. |
| Volume |
78 |
Issue |
2-4 |
Pages |
263-290 |
| Keywords |
Equine; Pony; Zebra; Donkey; Przewalski horse; Play behavior; Ethogram |
| Abstract |
An ethogram of play behavior among equids was developed. Several key English-language studies on equids were reviewed to derive a preliminary inventory of specific behaviors to be included in the ethogram. Our primary observations were based on a herd of semi-feral Shetland-type ponies kept at New Bolton Center, University of Pennsylvania School of Veterinary Medicine, Kennett Square, PA. Greater than 100 h of direct observation and photo-documentation focused specifically on play in order to identify play behaviors to be added to the preliminary inventory and to obtain detailed descriptions of each behavior. Additionally, these observations were supplemented with photographs obtained during several years of observational study of this herd for other purposes, and with the cumulative equid observational experience and study notes of the principal investigator with other equid species. An initial draft was sent out to 18 equine behavior colleagues for review. A total of 38 individual behaviors classified into four distinct categories were included in the ethogram. These included object play (14 entries), play sexual behavior (3 entries), locomotor play (14 entries) and play fighting (7 entries). All of the behaviors catalogued from direct observation of the herd were also found in the equid literature. The resulting ethogram offers a practical tool as a field guide or reference for quantitative research and other studies of equid play behavior as well as for teaching of equid behavior. |
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1987 |
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| Author |
Spengler M.I.; Rasia M. |
| Title |
Influence of Plasma Proteins on Erythrocyte Aggregation in Three Mammalian Species |
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Journal Article |
| Year |
2001 |
Publication |
Veterinary Research Communications |
Abbreviated Journal |
Vet.Res.Comm |
| Volume |
25 |
Issue |
7 |
Pages |
591-599 |
| Keywords |
albumin – bovine – equine – erythrocyte aggregation – dextran – haemorheology – human – plasma protein – polyvinylpyrrolidone |
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The aggregation capacity of human erythrocytes lies between that of the non-aggregating bovine erythrocytes and the remarkably aggregating equine ones. As the ability to aggregate is attributed to cell factors and the composition of the plasma proteins, the role that plasma proteins play in the aggregation process in these three species was studied. Washed erythrocytes were suspended in phosphate-buffered saline (PBS; pH 7.4, 300 mOsm/L) plus polyvinylpyrrolidone (PVP) in a suitable concentration to obtain an average intensity of aggregation (control media). The superimposed effect of replacing 80% of the medium by either autologous plasma, serum or albumin solution was studied. The plasma proteins appeared to enhance aggregation by human and equine erythrocytes, but impaired this process in bovine erythrocytes. Some evidence was obtained supporting the existence of serum factors capable of reducing aggregation of erythrocytes in cattle and it was concluded that the non-aggregating behaviour of bovine erythrocytes may be due to the cells interacting particularly with the macromolecules in the serum. |
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2013 |
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Mizuguchi, M.; Arai, M.; Ke, Y.; Nitta, K.; Kuwajima, K. |
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Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy |
Type |
Journal Article |
| Year |
1998 |
Publication |
Journal of Molecular Biology |
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283 |
Issue |
1 |
Pages |
265-277 |
| Keywords |
equine lysozyme; protein folding; molten globule; stopped-flow; folding intermediate |
| Abstract |
The equilibrium unfolding and the kinetics of unfolding and refolding of equine lysozyme, a Ca2+-binding protein, were studied by means of circular dichroism spectra in the far and near-ultraviolet regions. The transition curves of the guanidine hydrochloride-induced unfolding measured at 230 nm and 292.5 nm, and for the apo and holo forms of the protein have shown that the unfolding is well represented by a three-state mechanism in which the molten globule state is populated as a stable intermediate. The molten globule state of this protein is more stable and more native-like than that of α-lactalbumin, a homologous protein of equine lysozyme. The kinetic unfolding and refolding of the protein were induced by concentration jumps of the denaturant and measured by stopped-flow circular dichroism. The observed unfolding and refolding curves both agreed well with a single-exponential function. However, in the kinetic refolding reactions below 3 M guanidine hydrochloride, a burst-phase change in the circular dichroism was present, and the burst-phase intermediate in the kinetic refolding is shown to be identical with the molten globule state observed in the equilibrium unfolding. Under a strongly native condition, virtually all the molecules of equine lysozyme transform the structure from the unfolded state into the molten globule, and the subsequent refolding takes place from the molten globule state. The transition state of folding, which may exist between the molten globule and the native states, was characterized by investigating the guanidine hydrochloride concentration-dependence of the rate constants of refolding and unfolding. More than 80% of the hydrophobic surface of the protein is buried in the transition state, so that it is much closer to the native state than to the molten globule in which only 36% of the surface is buried in the interior of the molecule. It is concluded that all the present results are best explained by a sequential model of protein folding, in which the molten globule state is an obligatory folding intermediate on the pathway of folding. |
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3990 |
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