| Records |
| 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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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 Volume |
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Series Issue |
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Edition |
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| ISSN |
0042-4900 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:12498408 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
83 |
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| Author |
Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
| Title |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
Type |
Journal Article |
| Year |
2001 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
| Volume |
123 |
Issue |
27 |
Pages |
6649-6653 |
| Keywords |
Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
| Abstract |
We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding. |
| Address |
Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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English |
Summary Language |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0002-7863 |
ISBN |
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Conference |
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| Notes |
PMID:11439052 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3788 |
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| Author |
Keay, J.M.; Singh, J.; Gaunt, M.C.; Kaur, T. |
| Title |
Fecal glucocorticoids and their metabolites as indicators of stress in various mammalian species: a literature review |
Type |
Journal Article |
| Year |
2006 |
Publication |
Journal of zoo and wildlife medicine : official publication of the American Association of Zoo Veterinarians |
Abbreviated Journal |
J Zoo Wildl Med |
| Volume |
37 |
Issue |
3 |
Pages |
234-244 |
| Keywords |
Animals; *Animals, Wild/metabolism; Chromatography, High Pressure Liquid/methods/veterinary; Circadian Rhythm; Conservation of Natural Resources; *Ecosystem; Feces/*chemistry; Glucocorticoids/*analysis/metabolism; Humans; Seasons; Species Specificity; Specimen Handling/methods/veterinary; Stress, Psychological/*metabolism |
| Abstract |
Conservation medicine is a discipline in which researchers and conservationists study and respond to the dynamic interplay between animals, humans, and the environment. From a wildlife perspective, animal species are encountering stressors from numerous sources. With the rapidly increasing human population, a corresponding increased demand for food, fuel, and shelter; habitat destruction; and increased competition for natural resources, the health and well-being of wild animal populations is increasingly at risk of disease and endangerment. Scientific data are needed to measure the impact that human encroachment is having on wildlife. Nonbiased biometric data provide a means to measure the amount of stress being imposed on animals from humans, the environment, and other animals. The stress response in animals functions via glucocorticoid metabolism and is regulated by the hypothalamic-pituitary-adrenal axis. Fecal glucocorticoids, in particular, may be an extremely useful biometric test, since sample collection is noninvasive to subjects and, therefore, does not introduce other variables that may alter assay results. For this reason, many researchers and conservationists have begun to use fecal glucocorticoids as a means to measure stress in various animal species. This review article summarizes the literature on many studies in which fecal glucocorticoids and their metabolites have been used to assess stress levels in various mammalian species. Variations between studies are the main focus of this review. Collection methods, storage conditions, shipping procedures, and laboratory techniques utilized by different researchers are discussed. |
| Address |
Department of Biomedical Sciences and Pathobiology, Virginia-Maryland Regional College of Veterinary Medicine, Virginia Tech, 0442 Duck Pond Drive, Blacksburg, Virginia 24061, USA |
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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 Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
1042-7260 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:17319120 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
616 |
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| Author |
Gulotta, M.; Rogatsky, E.; Callender, R.H.; Dyer, R.B. |
| Title |
Primary folding dynamics of sperm whale apomyoglobin: core formation |
Type |
Journal Article |
| Year |
2003 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
| Volume |
84 |
Issue |
3 |
Pages |
1909-1918 |
| Keywords |
Animals; Apoproteins/*chemistry; Crystallography/*methods; Horses; Myocardium/chemistry; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Species Specificity; Structure-Activity Relationship; Temperature; Whales |
| Abstract |
The structure, thermodynamics, and kinetics of heat-induced unfolding of sperm whale apomyoglobin core formation have been studied. The most rudimentary core is formed at pH(*) 3.0 and up to 60 mM NaCl. Steady state for ultraviolet circular dichroism and fluorescence melting studies indicate that the core in this acid-destabilized state consists of a heterogeneous composition of structures of approximately 26 residues, two-thirds of the number involved for horse heart apomyoglobin under these conditions. Fluorescence temperature-jump relaxation studies show that there is only one process involved in Trp burial. This occurs in 20 micro s for a 7 degrees jump to 52 degrees C, which is close to the limits placed by diffusion on folding reactions. However, infrared temperature jump studies monitoring native helix burial are biexponential with times of 5 micro s and 56 micro s for a similar temperature jump. Both fluorescence and infrared fast phases are energetically favorable but the slow infrared absorbance phase is highly temperature-dependent, indicating a substantial enthalpic barrier for this process. The kinetics are best understood by a multiple-pathway kinetics model. The rapid phases likely represent direct burial of one or both of the Trp residues and parts of the G- and H-helices. We attribute the slow phase to burial and subsequent rearrangement of a misformed core or to a collapse having a high energy barrier wherein both Trps are solvent-exposed. |
| Address |
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA. gulotta@aecom.yu.edu |
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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 Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-3495 |
ISBN |
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Medium |
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Conference |
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| Notes |
PMID:12609893 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3783 |
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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 |
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 |
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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 Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-3002 |
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:1627604 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3800 |
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| Author |
Heistermann, M.; Palme, R.; Ganswindt, A. |
| Title |
Comparison of different enzyme-immunoassays for assessment of adrenocortical activity in primates based on fecal analysis |
Type |
Journal Article |
| Year |
2006 |
Publication |
American journal of primatology |
Abbreviated Journal |
Am. J. Primatol. |
| Volume |
68 |
Issue |
3 |
Pages |
257-273 |
| Keywords |
11-Hydroxycorticosteroids/*analysis; Adrenocorticotropic Hormone/pharmacology; Anesthesia; Animals; Corticosterone/analysis; Feces/*chemistry; Glucocorticoids/*analysis; Haplorhini/*metabolism; Hydrocortisone/analysis; Hypothalamo-Hypophyseal System/drug effects/physiology; Immunoenzyme Techniques/*methods; Pituitary-Adrenal System/drug effects/physiology; Species Specificity |
| Abstract |
Most studies published to date that used fecal glucocorticoid measurements to assess adrenocortical activity in primate (and many nonprimate) species applied a specific cortisol or corticosterone assay. However, since these native glucocorticoids are virtually absent in the feces of most vertebrates, including primates, the validity of this approach has recently been questioned. Therefore, the overall aim of the present study was to assess the validity of four enzyme-immunoassays (EIAs) using antibodies raised against cortisol, corticosterone, and reduced cortisol metabolites (two group-specific antibodies) for assessing adrenocortical activity using fecal glucocorticoid metabolite (GCM) measurements in selected primate species (marmoset, long-tailed macaque, Barbary macaque, chimpanzee, and gorilla). Using physiological stimulation of the hypothalamo-pituitary-adrenocortical (HPA) axis by administering exogenous ACTH or anesthesia, we demonstrated that at least two assays detected the predicted increase in fecal GCM levels in response to treatment in each species. However, the magnitude of response varied between assays and species, and no one assay was applicable to all species. While the corticosterone assay generally was of only limited suitability for assessing glucocorticoid output, the specific cortisol assay was valuable for those species that (according to high-performance liquid chromatography (HPLC) analysis data) excreted clearly detectable amounts of authentic cortisol into the feces. In contrast, in species in which cortisol was virtually absent in the feces, group-specific assays provided a much stronger signal, and these assays also performed well in the other primate species tested (except the marmoset). Collectively, the data suggest that the reliability of a given fecal glucocorticoid assay in reflecting activity of the HPA axis in primates clearly depends on the species in question. Although to date there is no single assay system that can be used successfully across species, our data suggest that group-specific assays have a high potential for cross-species application. Nevertheless, regardless of which GC antibody is chosen, our study clearly reinforces the necessity of appropriately validating the respective assay system before it is used. |
| Address |
Department of Reproductive Biology, German Primate Center, Gottingen, Germany. mheiste@gwdg.de |
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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 |
0275-2565 |
ISBN |
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Expedition |
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Conference |
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| Notes |
PMID:16477600 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4078 |
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| Author |
Touma, C.; Sachser, N.; Mostl, E.; Palme, R. |
| Title |
Effects of sex and time of day on metabolism and excretion of corticosterone in urine and feces of mice |
Type |
Journal Article |
| Year |
2003 |
Publication |
General and Comparative Endocrinology |
Abbreviated Journal |
Gen Comp Endocrinol |
| Volume |
130 |
Issue |
3 |
Pages |
267-278 |
| Keywords |
Animals; Chromatography, High Pressure Liquid; Circadian Rhythm/*physiology; Corticosterone/*metabolism/urine; Feces/*chemistry; Female; Immunoenzyme Techniques; Kinetics; Male; Mice; Mice, Inbred C57BL; Reference Values; Sex Factors; Stress/metabolism; Time Factors; Tritium |
| Abstract |
Non-invasive techniques to monitor stress hormones in small animals like mice offer several advantages and are highly demanded in laboratory as well as in field research. Since knowledge about the species-specific metabolism and excretion of glucocorticoids is essential to develop such a technique, we conducted radiometabolism studies in mice (Mus musculus f. domesticus, strain C57BL/6J). Each mouse was injected intraperitoneally with 740 kBq of 3H-labelled corticosterone and all voided urine and fecal samples were collected for five days. In a first experiment 16 animals (eight of each sex) received the injection at 9 a.m., while eight mice (four of each sex) were injected at 9 p.m. in a second experiment. In both experiments radioactive metabolites were recovered predominantly in the feces, although males excreted significantly higher proportions via the feces (about 73%) than females (about 53%). Peak radioactivity in the urine was detected within about 2h after injection, while in the feces peak concentrations were observed later (depending on the time of injection: about 10h postinjection in experiment 1 and about 4h postinjection in experiment 2, thus proving an effect of the time of day). The number and relative abundance of fecal [3H]corticosterone metabolites was determined by high performance liquid chromatography (HPLC). The HPLC separations revealed that corticosterone was extensively metabolized mainly to more polar substances. Regarding the types of metabolites formed, significant differences were found between males and females, but not between the experiments. Additionally, the immunoreactivity of these metabolites was assessed by screening the HPLC fractions with four enzyme immunoassays (EIA). However, only a newly established EIA for 5alpha-pregnane-3beta,11beta,21-triol-20-one (measuring corticosterone metabolites with a 5alpha-3beta,11beta-diol structure) detected several peaks of radioactive metabolites with high intensity in both sexes, while the other EIAs showed only minor immunoreactivity. Thus, our study for the first time provides substantial information about metabolism and excretion of corticosterone in urine and feces of mice and is the first demonstrating a significant impact of the animals' sex and the time of day. Based on these data it should be possible to monitor adrenocortical activity non-invasively in this species by measuring fecal corticosterone metabolites with the newly developed EIA. Since mice are extensively used in research world-wide, this could open new perspectives in various fields from ecology to behavioral endocrinology. |
| Address |
Department of Behavioral Biology, Institute of Neuro and Behavioral Biology, University of Muenster, Badestrasse 9, D-48149 Muenster, Germany. touma@uni-muenster.de |
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English |
Summary Language |
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Abbreviated Series Title |
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Edition |
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0016-6480 |
ISBN |
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| Notes |
PMID:12606269 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4086 |
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| Author |
Boucher, J.M.; Hanosset, R.; Augot, D.; Bart, J.M.; Morand, M.; Piarroux, R.; Pozet-Bouhier, F.; Losson, B.; Cliquet, F. |
| Title |
Detection of Echinococcus multilocularis in wild boars in France using PCR techniques against larval form |
Type |
Journal Article |
| Year |
2005 |
Publication |
Veterinary Parasitology |
Abbreviated Journal |
Vet Parasitol |
| Volume |
129 |
Issue |
3-4 |
Pages |
259-266 |
| Keywords |
Animals; Base Sequence; DNA, Helminth/chemistry/genetics; Echinococcosis/parasitology/pathology/*veterinary; Echinococcus multilocularis/*isolation & purification; Electron Transport Complex IV/chemistry/genetics; France; Histocytochemistry/veterinary; Liver/parasitology/pathology; Male; Molecular Sequence Data; Polymerase Chain Reaction/veterinary; Sequence Alignment; Sus scrofa/*parasitology; Swine Diseases/*parasitology/pathology |
| Abstract |
Recently, new data have been collected on the distribution and ecology of Echinococcus multilocularis in European countries. Different ungulates species such as pig, goat, sheep, cattle and horse are known to host incomplete development of larval E. multilocularis. We report a case of E. multilocularis portage in two wild boars from a high endemic area in France (Department of Jura). Histological examination was performed and the DNA was isolated from hepatic lesions then amplified by using three PCR methods in two distinct institutes. Molecular characterisation of PCR products revealed 99% nucleotide sequence homology with the specific sequence of the U1 sn RNA gene of E. multilocularis, 99 and 99.9% nucleotide sequence homology with the specific sequence of the cytochrome oxydase gene of Echinococcus genus and 99.9% nucleotide sequence homology with a genomic DNA sequence of Echinococcus genus for the first and the second wild boar, respectively. |
| Address |
AFSSA Nancy, Laboratoire d'Etudes et de Recherches sur la Rage et la Pathologie des Animaux Sauvages, Domaine de Pixerecourt-B.P. 9, Malzeville F 54220, France |
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English |
Summary Language |
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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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0304-4017 |
ISBN |
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| Notes |
PMID:15845281 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2629 |
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| Author |
Petter-Puchner, A.H.; Froetscher, W.; Krametter-Froetscher, R.; Lorinson, D.; Redl, H.; van Griensven, M. |
| Title |
The long-term neurocompatibility of human fibrin sealant and equine collagen as biomatrices in experimental spinal cord injury |
Type |
Journal Article |
| Year |
2007 |
Publication |
Experimental and Toxicologic Pathology : Official Journal of the Gesellschaft fur Toxikologische Pathologie |
Abbreviated Journal |
Exp Toxicol Pathol |
| Volume |
58 |
Issue |
4 |
Pages |
237-245 |
| Keywords |
Animals; Axotomy; Biocompatible Materials/*therapeutic use; Collagen/*therapeutic use; Fibrin Tissue Adhesive/*therapeutic use; Horses; Humans; Immunohistochemistry; Male; Motor Activity/physiology; Nerve Regeneration/*physiology; Rats; Recovery of Function; Spinal Cord/pathology/physiology; Spinal Cord Injuries/pathology/*therapy; Thoracic Vertebrae |
| Abstract |
INTRODUCTION: While fibrin sealant (FS) and equine collagen (EC) have been used as scaffold materials in experimental spinal cord injury (SCI), questions concerning neurocompatibility still remain. In this study, we assessed potential adverse effects, as well as functional and histological impact of FS and EC in subtotal hemisection of the thoracic spinal cord (SC) in rats. METHODS: 124 male rats were randomly assigned to four main groups (n=31): Sham (SH), Lesion only (L), fibrin sealant (GFS) and equine collagen group (GEC). SH animals received laminectomy only; all other animals underwent subtotal lateral hemisection at T9. Treatment consisted of application of FS or EC into the lesion gap in GFS and GEC, which was left empty in L. GFS, GEC, L and SH were each further divided into 4 subgroups: One subgroup, consisting of 10 rats was subjected to behavioural and reflex testing before surgery and followed up on days 1,7, 14, 21, 28 post op and then sacrificed. Haemalaun or cresyl violet (CV) was used to identify neutrophils in parasagittal cord sections which were obtained on day 1 (n=7). Sections stained for quantification of microglia/macrophages using ED-1 on day 3 (n=7), day 7 (n=7) and day 28 (n=7 out of 10). Additionally, neural filament (NF) staining was chosen to detect axonal regeneration and the length of ingrowth into FS and EC, Luxol blue for myelination, Von Willebrand factor for vascularisation, and glial fibrillary acidic protein (GFAP) staining for detection of astrocytes in glial scars on day 28. RESULTS: No adverse effects were observed in the treatment groups. Compared to L, GFS and GEC performed significantly better in the Basso, Beattie, Bresnahan (BBB) score and hopping responses. Proprioceptive placing was markedly improved in FS and EC compared to L. Axonal regrowth was found in GFS and GEC--the regrowth in the GFS was accompanied by myelination and vascularisation. Glial scarring occurred in all groups. Discussion Both biomatrices improved functional recovery compared to L and no adverse effects were perceived. |
| Address |
Ludwig Boltzmann Institute of Experimental and Clinical Traumatology, Donaueschingenstrasse 13, 1200-Vienna, Austria |
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English |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0940-2993 |
ISBN |
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| Notes |
PMID:17118635 |
Approved |
no |
| Call Number |
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Serial |
1852 |
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| Author |
Permyakov, S.E.; Khokhlova, T.I.; Nazipova, A.A.; Zhadan, A.P.; Morozova-Roche, L.A.; Permyakov, E.A. |
| Title |
Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature “phase diagrams” |
Type |
Journal Article |
| Year |
2006 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
| Volume |
65 |
Issue |
4 |
Pages |
984-998 |
| Keywords |
Animals; Apoproteins/chemistry/metabolism; Binding Sites; Calcium/chemistry/*metabolism; Cattle; Edetic Acid/metabolism; Horses/metabolism; Hydrogen-Ion Concentration; Lactalbumin/chemistry/metabolism; Muramidase/*chemistry/*metabolism; Protein Denaturation; Spectrometry, Fluorescence; *Temperature; Thermodynamics; Tryptophan/chemistry/metabolism |
| Abstract |
The most universal approach to the studies of metal binding properties of single-site metal binding proteins, i.e., construction of a “phase diagram” in coordinates of free metal ion concentration-temperature, has been applied to equine lysozyme (EQL). EQL has one relatively strong calcium binding site and shows two thermal transitions, but only one of them is Ca(2+)-dependent. It has been found that the Ca(2+)-dependent behavior of the low temperature thermal transition (I) of EQL can be adequately described based upon the simplest four-states scheme of metal- and temperature-induced structural changes in a protein. All thermodynamic parameters of this scheme were determined experimentally and used for construction of the EQL phase diagram in the pCa-temperature space. Comparison of the phase diagram with that for alpha-lactalbumin (alpha-LA), a close homologue of lysozyme, allows visualization of the differences in thermodynamic behavior of the two proteins. The thermal stability of apo-EQL (transition I) closely resembles that for apo-alpha-LA (mid-temperature 25 degrees C), while the thermal stabilities of their Ca(2+)-bound forms are almost indistinguishable. The native state of EQL has three orders of magnitude lower affinity for Ca(2+) in comparison with alpha-LA while its thermally unfolded state (after the I transition) has about one order lower (K = 15M(-1)) affinity for calcium. Circular dichroism studies of the apo-lysozyme state after the first thermal transition show that it shares common features with the molten globule state of alpha-LA. |
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Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow region 142290, Russia |
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English |
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1097-0134 |
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PMID:17022083 |
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1858 |
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