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Author |
Granquist,S.M.; Sigurjónsdóttir, H; Thórhallsdóttir, A.G. |
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Title |
Social structure and interactions within groups of horses containing a stallion |
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Conference Article |
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Year |
2008 |
Publication |
IESM 2008 |
Abbreviated Journal |
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Keywords |
Social interactions,, Stallions, Hierarchy, Icelandic horses |
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Abstract  |
Earlier research indicates that stallions might either prevent social interactions between mares in their
herds directly or indirectly by their presence (Feist and McCullough, 1976; Sigurjonsdottir et al.,
2003) The impact of stallions on the social interactions between harem members was studied in 6
groups of Icelandic horses in 2004, 2006 and 2007 for altogether 525 hours. Four of the groups were
permanently living together under semi-feral conditions, while two were temporary breeding groups. In
addition, temporary and permanent groups were compared and the effect of the stability of the group
on the social behaviour of horses was investigated .
The results show that stallions seldom intervene directly in social interactions between harem
members. However, the hierarchies were less rigid and fewer friendship bonds were found in the
groups compared to what has been found in groups without stallions in Iceland. These results give
some support to our prediction that the stallion does indirectly suppress social interactions of herd
members.
The stability of the group was found to affect the aggression rate, since a higher aggression rate was
found in the temporary groups compared to the permanent groups. The number of preferred
allogrooming partners of the horses was also affected to some extent, as a significantly lower number
of allogrooming partners was found in the most unstable group compared to all the other groups. The
results have significance for further research in the field of social structure of mammals, and may also
be applied in the management of horses and other domestic animals. |
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Sigurjónsdóttir, H |
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IESM 2008 |
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Notes |
Talk 15 min IESM 2008 Fullpaper |
Approved |
yes |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4487 |
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Author |
Crans, W.J.; McNelly, J.; Schulze, T.L.; Main, A. |
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Title |
Isolation of eastern equine encephalitis virus from Aedes sollicitans during an epizootic in southern New Jersey |
Type |
Journal Article |
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Year |
1986 |
Publication |
Journal of the American Mosquito Control Association |
Abbreviated Journal |
J Am Mosq Control Assoc |
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Volume |
2 |
Issue |
1 |
Pages |
68-72 |
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Keywords |
Aedes/*microbiology; Alphavirus/*isolation & purification; Animals; Disease Outbreaks/veterinary; Ecology; Encephalitis Virus, Eastern Equine/*isolation & purification; Encephalomyelitis, Equine/epidemiology/transmission/veterinary; Horse Diseases/epidemiology/transmission; Horses; Insect Vectors/microbiology; New Jersey |
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Abstract |
Eastern equine encephalitis virus (EEE) was isolated from the salt marsh mosquito, Aedes sollicitans, collected from coastal areas of New Jersey on 3 occasions during the late summer and fall of 1982. The isolations were made at a time when local Culiseta melanura were either undergoing a population increase or exhibiting high levels of EEE virus. Although no human cases were reported during the epizootic period, the data lend support to the hypothesis that Ae. sollicitans is capable of functioning as an epidemic vector in the coastal areas of New Jersey where human cases of EEE have been most common. |
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Mosquito Research and Control, Cook College, Rutgers University, New Brunswick, NJ 08903 |
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8756-971X |
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PMID:2853203 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2684 |
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Author |
Kida, H. |
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Title |
[Ecology of influenza viruses in animals and the mechanism of emergence of new pandemic strains] |
Type |
Journal Article |
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Year |
1997 |
Publication |
Nippon Rinsho. Japanese Journal of Clinical Medicine |
Abbreviated Journal |
Nippon Rinsho |
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Volume |
55 |
Issue |
10 |
Pages |
2521-2526 |
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Keywords |
Animals; Bird Diseases/transmission; Birds; Horse Diseases/transmission; Horses; Humans; Influenza, Human/transmission/*veterinary; Swine; Swine Diseases/transmission; Zoonoses |
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Abstract |
Ecological studies on influenza viruses revealed that the hemagglutinin genes are introduced into new pandemic strains from viruses circulating in migratory ducks through domestic ducks and pigs in southern China. Experimental infection of pigs with 38 avian influenza virus strains with H1-H13 hemagglutinins showed that at least one strain of each HA subtype replicated in the upper respiratory tract of pigs. Co-infection of pigs with a swine virus and with an avian virus generated reassortant viruses. The results indicate that avian viruses of any subtype can contribute genes in the generation of reassortants. Virological surveillance revealed that influenza viruses in waterfowl reservoir are perpetuated year-by-year in the frozen lake water while ducks are absent. |
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Department of Disease Control, Hokkaido University Graduate School of Veterinary Medicine |
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Japanese |
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ISSN |
0047-1852 |
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Notes |
PMID:9360367 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2654 |
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Author |
Hirota, S.; Suzuki, M.; Watanabe, Y. |
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Title |
Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c |
Type |
Journal Article |
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Year |
2004 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
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Volume |
314 |
Issue |
2 |
Pages |
452-458 |
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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 |
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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. |
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Address |
Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp |
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0006-291X |
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Notes |
PMID:14733927 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3777 |
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Author |
Jablonska, E.M.; Ziolkowska, S.M.; Gill, J.; Szykula, R.; Faff, J. |
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Title |
Changes in some haematological and metabolic indices in young horses during the first year of jump-training |
Type |
Journal Article |
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Year |
1991 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
23 |
Issue |
4 |
Pages |
309-311 |
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Keywords |
Alanine Transaminase/blood; Animals; Bicarbonates/blood; Blood Glucose/analysis; Blood Proteins/analysis; Breeding; Carbon Dioxide/blood; Exercise Test/veterinary; Fatty Acids, Nonesterified/blood; Female; Fructose-Bisphosphate Aldolase/blood; Hematocrit/veterinary; Hemoglobins/analysis; Horses/*blood/metabolism; Hydrogen-Ion Concentration; Lactates/blood; Male; Oxygen/blood; *Physical Conditioning, Animal; Pyruvates/blood |
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Abstract |
Effects of an 18 min exercise test, on three separate occasions during a one year jump-training programme, was studied in seven horses. Determinations were carried out on venous blood for packed cell volume, haemoglobin, total protein, lactate and pyruvate, glucose, free fatty acids, insulin, glucagon, blood gases, bicarbonate, pH, aldolase, aspartate aminotransferase and alanine amino-transferase. Exercise caused a slight increase in lactate and pyruvate, total protein, aldolase, alanine aminotransferase, pO2, bicarbonate and pH. Glucose, free fatty acids and pCO2 levels decreased. Training caused no significant difference in these changes. However, during the year, increases in lactate and decreases in pH (resting levels) were observed. |
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Department of Vertebrate Animal Physiology, Warszawa, Poland |
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ISSN |
0425-1644 |
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Notes |
PMID:1915234 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3801 |
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Author |
Gatta, D.; Baragli, P.; Ferrarini, N.; Ciattini, F.; Sighieri, C.; Colombani, B. |
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Title |
Fitness evaluation in endurance horses by standardised exercise test on treadmill |
Type |
Journal Article |
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Year |
1998 |
Publication |
Ippologia |
Abbreviated Journal |
Valutazione dello stato di allenamento del cavallo da endurance mediante test standardizzato su trea |
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Volume |
9 |
Issue |
4 |
Pages |
57-69 |
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Keywords |
Endurance; Horses; Treadmill |
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Abstract |
Endurance horses, like marathon runners, undertake sub-maximal, longterm physical exercises and in both cases thermoregulation plays a critical role. A standardised sub-maximal treadmill test was used to assess fitness and training state in endurance horses. Literature reports that trained human athletes dissipate head load better than not trained ones; in this study parameters related to thermoregulation were recorded together with other haematologic and metabolic ones. Six endurance horses, divided into two groups according to their training state, performed two submaximal tests at a distance of one week. Blood samples were collected at rest, during exercise, at the end and during recovery (10, 30 and 60 minutes after work). Heart rate (HR), respiratory rate (RR), rectal (RT) and skin (ST) temperatures were monitored through the exercise (and recovery for HR). HR resulted significantly lower (P<0.01) in trained horses than in untrained ones, especially during recovery. Also rectal and skin temperatures resulted significantly lower (P<0.05) in trained horses and ST increased more gradually during exercise. The values of haematocrit and haemoglobin resulted significantly lower (P<0.05) at rest, during exercise and recovery samples. In this study, the parameters related to thermoregulation, in accordance with data from human athletes, resulted significantly different in trained and untrained horses, while other parameters didn't vary significantly between the two groups. Thermoregulatory responses to exercise-generated heat load in a standardised test, studied by simple parameters, can thus offer useful information about fitness and training state of endurance horses. |
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Address |
Dipto. Anat., Biochim. Fisiol. Vet., Univ. degli Studi di Pisa |
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Notes |
Cited By (since 1996): 2; Export Date: 13 November 2008; Source: Scopus |
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Equine Behaviour @ team @ |
Serial |
4655 |
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Author |
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
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Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
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Journal Article |
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Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
113 |
Issue |
3 |
Pages |
425-433 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism |
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Abstract |
Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion. |
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0014-2956 |
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PMID:7011796 |
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Equine Behaviour @ team @ |
Serial |
3810 |
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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 |
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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 |
Traversa, D.; Otranto, D.; Iorio, R.; Giangaspero, A. |
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Title |
Molecular characterization of Thelazia lacrymalis (Nematoda, Spirurida) affecting equids: a tool for vector identification |
Type |
Journal Article |
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Year |
2005 |
Publication |
Molecular and Cellular Probes |
Abbreviated Journal |
Mol Cell Probes |
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Volume |
19 |
Issue |
4 |
Pages |
245-249 |
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Keywords |
Animals; Horse Diseases/parasitology; Horses/*parasitology; Insect Vectors/*parasitology; Muscidae/*parasitology; Polymerase Chain Reaction; Polymorphism, Restriction Fragment Length; Spirurida Infections/parasitology/veterinary; Thelazioidea/chemistry/*genetics |
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Abstract |
Equine thelaziosis caused by the eyeworm Thelazia lacrymalis is a parasitic disease transmitted by muscid flies. Although equine thelaziosis is known to have worldwide distribution, information on the epidemiology and presence of the intermediate hosts of T. lacrymalis is lacking. In the present work, a PCR-RFLP based assay on the first and/or second internal transcribed spacer (ITS1 and ITS2) of ribosomal DNA was developed for the detection of T. lacrymalis DNA in its putative vector(s). The sensitivity of the technique was also assessed. The restriction patterns obtained readily differentiated T. lacrymalis from four species of Musca (Diptera, Muscidae) (i.e. Musca autumnalis, Musca domestica, Musca larvipara and Musca osiris), which are potential vectors of equine eyeworms. The molecular assay presented herein is a useful tool to identify the intermediate host(s) of T. lacrymalis in natural conditions and to study its/their ecology and epidemiology. |
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Address |
Department of Biomedical Comparative Sciences, Faculty of Veterinary Medicine, University of Teramo, Piazza Aldo Moro 45, 64100 Teramo, Italy. dtraversa@unite.it |
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0890-8508 |
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PMID:16038792 |
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Equine Behaviour @ team @ |
Serial |
2626 |
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Author |
Hodgson, D.; Howe, S.; Jeffcott, L.; Reid, S.; Mellor, D.; Higgins, A. |
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Title |
Effect of prolonged use of altrenogest on behaviour in mares |
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Year |
2005 |
Publication |
Veterinary journal (London, England : 1997) |
Abbreviated Journal |
Vet J |
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Volume |
169 |
Issue |
1 |
Pages |
113-115 |
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Keywords |
Administration, Oral; Anabolic Agents/adverse effects/*pharmacology; Animals; Behavior, Animal/*drug effects; Body Constitution/drug effects; Body Weight/drug effects; *Doping in Sports; Female; Horses/*physiology; Social Behavior; Social Dominance; Time Factors; Trenbolone/adverse effects/*analogs & derivatives/*pharmacology |
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Abstract |
Erratum in:
Vet J. 2005 May;169(3):321.
Corrected and republished in:
Vet J. 2005 May;169(3):322-5.
Oral administration of altrenogest for oestrus suppression in competition horses is believed to be widespread in some equestrian disciplines, and can be administered continuously for several months during a competition season. To examine whether altrenogest has any anabolic or other potential performance enhancing properties that may give a horse an unfair advantage, we examined the effect of oral altrenogest (0.044 mg/kg), given daily for a period of eight weeks, on social hierarchy, activity budget, body-mass and body condition score of 12 sedentary mares. We concluded that prolonged oral administration of altrenogest at recommended dose rates to sedentary mares resulted in no effect on dominance hierarchies, body mass or condition score. |
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Address |
Faculty of Veterinary Science, University of Sydney, Private Mailbag 4, Narellan Delivery Centre, Narellan, NSW 2567, Australia. davidh@camden.usyd.edu.au |
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1090-0233 |
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PMID:15683772 |
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Call Number |
refbase @ user @ |
Serial |
671 |
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