| Records |
| Author |
Elsaesser, F.; Klobasa, F.; Ellendorff, F. |
| Title |
ACTH stimulation test for the determination of salivary cortisol and of cortisol responses as markers of the training status/fitness of warm-blooded sports horses] |
Type |
Journal Article |
| Year |
2001 |
Publication |
DTW. Deutsche Tierarztliche Wochenschrift |
Abbreviated Journal |
Dtsch Tierarztl Wochenschr |
| Volume |
108 |
Issue |
1 |
Pages |
31-36 |
Keywords  |
Adrenocorticotropic Hormone/*diagnostic use; Animals; Health; Horses/*physiology; Hydrocortisone/*analysis/*secretion; Male; Orchiectomy; *Physical Conditioning, Animal; Running; Saliva/*chemistry; Walking |
| Abstract |
Previous work (Marc et al., 2000) suggested that plasma cortisol responses to treadmill exercise or ACTH injection are a reliable marker for performance evaluation in warmblood horses. For practical purposes blood sample collections and treadmill exercise tests are somewhat troublesome and time consuming. The goal of this study was thus to evaluate the use of saliva for cortisol determination (by direct EIA) as a marker for performance and to investigate the reliability and repeatability of plasma cortisol responses to a single i.v. injection of ACTH (50 micrograms or 250 micrograms). Furthermore, the effect of training horses for 8 weeks 3 times per week covering the same distance (increasing from 3.5 km during the first week to 8 km during the last week) either by trotting (approximately 240 m/min) or by cantering (375 m/min) was investigated. For this purpose initially ten four-year-old Hannovarian geldings, all reared in the same State stud, were used. Mean overall correlation between salivary cortisol and plasma cortisol concentrations was 0.64 when samples of various points of time were used. However, in spite of attempts to standardize saliva sample collection, correlation between salivary cortisol levels and plasma cortisol levels at distinct points of time in different tests were low and significant (r = 0.85, p < 0.02) only in one test. Thus, salivary cortisol measurements for diagnostic purposes are not reliable or useful. The repeatability of plasma cortisol responses to ACTH for untrained and trained horses were r = 0.86 and r = 0.8 respectively (p < or = 0.01 and p < or = 0.05 respectively). Training horses either by trotting or cantering did not affect the cortisol response either to treadmill exercise or to stimulation by ACTH. It is concluded that the relationship between salivary cortisol levels and plasma cortisol levels is not close enough to allow the use of salivary cortisol determination as marker of the training status/fitness of horses. The repeatability of the cortisol response to ACTH is similar to the cortisol response to treadmill exercise. Based on plasma cortisol responses to ACTH or treadmill exercise training horses by cantering at low speed is not superior to training by trotting for the fitness of horses. |
| Address |
Institut fur Tierzucht und Tierverhalten Mariensee (FAL), Holtystrasse 10, 31535 Neustadt. elsaesser@tzv.fal.de |
| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
German |
Summary Language |
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Original Title |
ACTH Stimulationstest und Bestimmung von Cortisol im Blut und Speichel zur Bewertung des Trainingszustands/der Kondition beim Warmblutpferd |
| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
|
| ISSN |
0341-6593 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:11232423 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4053 |
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| Author |
Thiel, D.; Jenni-Eiermann, S.; Palme, R. |
| Title |
Measuring corticosterone metabolites in droppings of capercaillies (Tetrao urogallus) |
Type |
Journal Article |
| Year |
2005 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
| Volume |
1046 |
Issue |
|
Pages |
96-108 |
| Keywords |
Adrenocorticotropic Hormone/administration & dosage/analysis/metabolism; Animals; Circadian Rhythm; Corticosterone/administration & dosage/*analysis/*metabolism; Feces/*chemistry; Female; Freezing; Galliformes/*metabolism; Male; Reproducibility of Results; Sex Factors; Temperature; Time Factors; Tritium/diagnostic use |
| Abstract |
The capercaillie (Tetrao urogallus), the largest grouse species in the world, is decreasing in numbers in major parts of its distribution range. Disturbances by human outdoor activities are discussed as a possible reason for this population decline. An indicator for disturbances is the increase of the glucocorticoid corticosterone, a stress hormone, which helps to cope with life-threatening situations. However, repeated disturbances might result in a long-term increase of the basal corticosterone concentration, which can result in detrimental effects like reduced fitness and survival of an animal. To measure corticosterone metabolites (CMs) noninvasively in the droppings of free-living capercaillies, first an enzyme immunoassay (EIA) in captive birds had to be selected and validated. Therefore, the excretion pattern of intravenously injected radiolabeled corticosterone was determined and 3H metabolites were characterized. High-performance liquid chromatography (HPLC) separations of the samples containing peak concentrations revealed that corticosterone was extensively metabolized. The HPLC fractions were tested in several EIAs for glucocorticoid metabolites. The physiological relevance of this method was proved after pharmacological stimulation of the adrenocortical activity. Only the recently established cortisone assay, measuring CMs with a 3,11-dione structure, detected an expressed increase of concentrations following ACTH stimulation. To set up a sampling protocol suited for the field, we examined the influence of various storage conditions and time of day on concentrations of CMs. |
| Address |
Swiss Ornithological Institute, 6204 Sempach, Switzerland. dominik.thiel@vogelwarte.ch |
| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0077-8923 |
ISBN |
|
Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:16055846 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4079 |
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| |
| Author |
Baltic, M.; Jenni-Eiermann, S.; Arlettaz, R.; Palme, R. |
| Title |
A noninvasive technique to evaluate human-generated stress in the black grouse |
Type |
Journal Article |
| Year |
2005 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
| Volume |
1046 |
Issue |
|
Pages |
81-95 |
| Keywords |
Adrenocorticotropic Hormone/metabolism; Animals; Bird Diseases/*metabolism; Conservation of Natural Resources; Corticosterone/*metabolism; Ecosystem; Feces/*chemistry; Female; Galliformes/*metabolism; Immunoenzyme Techniques/methods/veterinary; Male; Reproducibility of Results; Stress/metabolism/*veterinary; Tritium/diagnostic use |
| Abstract |
The continuous development of tourism and related leisure activities is exerting an increasingly intense pressure on wildlife. In this study, a novel noninvasive method for measuring stress in the black grouse, an endangered, emblematic species of European ecosystems that is currently declining in several parts of its European range, is tested and physiologically validated. A radiometabolism study and an ACTH challenge test were performed on four captive black grouse (two of each sex) in order to get basic information about the metabolism and excretion of corticosterone and to find an appropriate enzyme-immunoassay (EIA) to measure its metabolites in the feces. Peak radioactivity in the droppings was detected within 1 to 2 hours. Injected (3)H-corticosterone was excreted as polar metabolites and by itself was almost absent. A cortisone-EIA was chosen from among seven tested EIAs for different groups of glucocorticoid metabolites, because it cross-reacted with some of the formed metabolites and best reflected the increase of excreted corticosterone metabolites, after the ACTH challenge test. Concentrations of the metabolites from fecal samples collected from snow burrows of free-ranging black grouse were within the same range as in captive birds. The noninvasive method described may be appropriate for evaluating the stress faced by free-living black grouse populations in the wild, particularly in mountain ecosystems where human disturbance, especially by winter sports, is of increasing conservation concern. |
| Address |
Zoological Institute, Division of Conservation Biology, Baltzerstrasse 6, CH-3012 Bern, Switzerland |
| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0077-8923 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:16055845 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4080 |
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| Author |
Pierce, M.M.; Nall, B.T. |
| Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
Type |
Journal Article |
| Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
| Volume |
298 |
Issue |
5 |
Pages |
955-969 |
| 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 |
| Abstract |
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. |
| Address |
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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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0022-2836 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:10801361 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
3853 |
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| Author |
Yokoyama, S.; Radlwimmer, F.B. |
| Title |
The molecular genetics of red and green color vision in mammals |
Type |
Journal Article |
| Year |
1999 |
Publication |
Genetics |
Abbreviated Journal |
Genetics |
| Volume |
153 |
Issue |
2 |
Pages |
919-932 |
| Keywords |
Amino Acid Sequence; Animals; Base Sequence; COS Cells; Cats; Color Perception/*genetics; DNA Primers; Deer; Dolphins; *Evolution, Molecular; Goats; Guinea Pigs; Horses; Humans; Mammals/*genetics/physiology; Mice; Molecular Sequence Data; Opsin/biosynthesis/chemistry/*genetics; *Phylogeny; Rabbits; Rats; Recombinant Proteins/biosynthesis; Reverse Transcriptase Polymerase Chain Reaction; Sciuridae; Sequence Alignment; Sequence Homology, Amino Acid; Transfection |
| Abstract |
To elucidate the molecular mechanisms of red-green color vision in mammals, we have cloned and sequenced the red and green opsin cDNAs of cat (Felis catus), horse (Equus caballus), gray squirrel (Sciurus carolinensis), white-tailed deer (Odocoileus virginianus), and guinea pig (Cavia porcellus). These opsins were expressed in COS1 cells and reconstituted with 11-cis-retinal. The purified visual pigments of the cat, horse, squirrel, deer, and guinea pig have lambdamax values at 553, 545, 532, 531, and 516 nm, respectively, which are precise to within +/-1 nm. We also regenerated the “true” red pigment of goldfish (Carassius auratus), which has a lambdamax value at 559 +/- 4 nm. Multiple linear regression analyses show that S180A, H197Y, Y277F, T285A, and A308S shift the lambdamax values of the red and green pigments in mammals toward blue by 7, 28, 7, 15, and 16 nm, respectively, and the reverse amino acid changes toward red by the same extents. The additive effects of these amino acid changes fully explain the red-green color vision in a wide range of mammalian species, goldfish, American chameleon (Anolis carolinensis), and pigeon (Columba livia). |
| Address |
Department of Biology, Syracuse University, Syracuse, New York 13244, USA. syokoyam@mailbox.syr.edu |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0016-6731 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:10511567 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4063 |
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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 |
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 |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-291X |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:14733927 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3777 |
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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 |
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 |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0021-9673 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:17196214 |
Approved |
no |
| Call Number |
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Serial |
1842 |
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| Author |
Selby, L.A.; Marienfeld, C.J.; Pierce, J.O. |
| Title |
The effects of trace elements on human and animal health |
Type |
Journal Article |
| Year |
1970 |
Publication |
Journal of the American Veterinary Medical Association |
Abbreviated Journal |
J Am Vet Med Assoc |
| Volume |
157 |
Issue |
11 |
Pages |
1800-1808 |
| Keywords |
Anemia, Hypochromic/veterinary; Animal Nutrition Physiology; Animals; Artiodactyla/*physiology; Chemistry; Cobalt/analysis/metabolism; Copper/analysis/metabolism; Deficiency Diseases/veterinary; Dogs/*physiology; Ecology; Horses/*physiology; Humans; Iodine/analysis/metabolism; Iron/analysis/metabolism; Manganese/analysis/metabolism; Nutritional Requirements; Selenium/metabolism; Trace Elements/*metabolism; Zinc/analysis/metabolism |
| Abstract |
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| Address |
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Thesis |
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Place of Publication |
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Editor |
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English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0003-1488 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:4922190 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2733 |
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| Author |
Husted, L.; Andersen, M.S.; Borggaard, O.K.; Houe, H.; Olsen, S.N. |
| Title |
Risk factors for faecal sand excretion in Icelandic horses |
Type |
Journal Article |
| Year |
2005 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
| Volume |
37 |
Issue |
4 |
Pages |
351-355 |
| Keywords |
Animal Feed; Animal Husbandry/methods; Animals; Denmark; Feces/*chemistry; Female; Gastrointestinal Diseases/epidemiology/etiology/prevention & control/veterinary; Horse Diseases/epidemiology/etiology/prevention & control; Horses/*metabolism; Logistic Models; Male; Pilot Projects; *Poaceae/growth & development; Risk Factors; Silicon Dioxide/administration & dosage/adverse effects/*analysis; Soil/*analysis |
| Abstract |
REASONS FOR PERFORMING STUDY: Sandy soil is often mentioned as a risk factor in the development of sand-related gastrointestinal disease (SGID) in the horse. There are other variables, but few studies confirm any of these. OBJECTIVE: To investigate soil type, pasture quality, feeding practice in the paddock, age, sex and body condition score as risk factors for sand intake in the horse. METHODS: Faeces were collected from 211 Icelandic horses on 19 different studs in Denmark together with soil samples and other potential risk factors. Sand content in faeces determined by a sand sedimentation test was interpreted as evidence of sand intake. Soil types were identified by soil analysis and significance of the data was tested using logistic analysis. RESULTS: Of horses included in the study, 56.4% showed sand in the faeces and 5.7% had more than 5 mm sand as quantified by the rectal sleeve sedimentation test. Soil type had no significant effect when tested as main effect, but there was interaction between soil type and pasture quality. Significant interactions were also found between paddock feeding practice and pasture quality. CONCLUSION: To evaluate the risk of sand intake it is important to consider 3 variables: soil type, pasture quality and feeding practice. Pasture quality was identified as a risk factor of both short and long grass in combination with sandy soil, while clay soil had the lowest risk in these combinations. Feeding practice in the paddock revealed feeding directly on the ground to be a risk factor when there was short (1-5 cm) or no grass. Also, no feeding outdoors increased the risk on pastures with short grass, while this had no effect in paddocks with no grass. More than 50% of all horses investigated in this study had sand in the faeces. POTENTIAL RELEVANCE: The identification of risk factors is an important step towards prevention of SGID. Further research is necessary to determine why some horses exhibit more than 5 mm sand in the sedimentation test and whether this is correlated with geophagic behaviour. |
| Address |
Department of Large Animal Sciences, The Royal Veterinary and Agricultural University, Dyrlaegevej 88, DK-1870 Frederiksberg, Denmark |
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Place of Publication |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0425-1644 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:16028626 |
Approved |
no |
| Call Number |
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Serial |
1888 |
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| Author |
Nicol, C.J.; Davidson, H.P.D.; Harris, P.A.; Waters, A.J.; Wilson, A.D. |
| Title |
Study of crib-biting and gastric inflammation and ulceration in young horses |
Type |
Journal Article |
| Year |
2002 |
Publication |
The Veterinary record |
Abbreviated Journal |
Vet. Rec. |
| Volume |
151 |
Issue |
22 |
Pages |
658-662 |
| Keywords |
Animal Husbandry/methods; Animals; Antacids/therapeutic use; *Behavior, Animal; Diet/veterinary; Endoscopy, Gastrointestinal/veterinary; Feces/chemistry; Female; Gastritis/diet therapy/physiopathology/*veterinary; Horse Diseases/diet therapy/*physiopathology/psychology; Horses; Hydrogen-Ion Concentration; Male; Random Allocation; Stereotyped Behavior/*physiology; Stomach Ulcer/diet therapy/physiopathology/*veterinary; Treatment Outcome; Weaning |
| Abstract |
Nineteen young horses that had recently started to perform the stereotypy of crib-biting were compared with 16 non-stereotypic horses for 14 weeks. After initial observations of their behaviour and an endoscopic examination of the condition of their stomachs, the horses were randomly allocated to a control or an antacid diet At the start of the trial, the stomachs of the crib-biting foals were significantly more ulcerated and inflamed than the stomachs of the normal foals. In addition, the faecal pH of the crib-biting foals (6.05) was significantly lower than that of the normal foals (6.58). The antacid diet resulted in a significant improvement in the condition of the horses' stomachs. The crib-biting behaviour declined in most of the foals, regardless of their diet, but tended to decline to a greater extent in the foals on the antacid diet. |
| Address |
Department of Clinical Veterinary Science, University of Bristol, Langford House, Bristol BS40 5DU |
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Place of Publication |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
0042-4900 |
ISBN |
|
Medium |
|
| Area |
|
Expedition |
|
Conference |
|
| Notes |
PMID:12498408 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
83 |
| Permanent link to this record |
