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	Author	Natalini, C.C.; Robinson, E.P.
	Title	Effects of epidural opioid analgesics on heart rate, arterial blood pressure, respiratory rate, body temperature, and behavior in horses			Type	Journal Article
	Year	2003	Publication	Veterinary Therapeutics : Research in Applied Veterinary Medicine	Abbreviated Journal	Vet Ther
	Volume	4	Issue	4	Pages	364-375
	Keywords	3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer/administration & dosage/pharmacology; Alfentanil/administration & dosage/pharmacology; Analgesics, Opioid/administration & dosage/pharmacology; Anesthesia, Epidural/veterinary; Animals; Behavior, Animal/drug effects; Blood Pressure/drug effects; Body Temperature/drug effects; Butorphanol/administration & dosage/pharmacology; Cross-Over Studies; Female; Heart Rate/drug effects; Horses/*physiology; Injections, Epidural/veterinary; Male; Morphine/administration & dosage/pharmacology; Respiration/drug effects; Tramadol/administration & dosage/pharmacology
	Abstract	Heart rate, arterial blood pressures, respiratory rate, body temperature, and central nervous system excitement were compared before and after epidural administration of morphine (0.1 mg/kg), butorphanol (0.08 mg/kg), alfentanil (0.02 mg/kg), tramadol (1.0 mg/kg), the k-opioid agonist U50488H (0.08 mg/kg), or sterile water using an incomplete Latin square crossover design in five conscious adult horses. Treatments were administered into the first intercoccygeal epidural space. Significant (P <.05) reductions in respiratory rate were detected after epidural administration of morphine, alfentanil, U50488H, and sterile water. Additionally, significant (P <.05) head ptosis was observed within the first hour after administration of morphine, U50488H, and tramadol, but neither of these changes appeared to be of clinical significance. No treatment-related changes in motor activity or behavior were observed.
	Address	Department of Veterinary Clinical Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, USA
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	1528-3593	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:15136978			Approved	no
	Call Number				Serial	1902
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	Author	Marlin, D.J.; Schroter, R.C.; White, S.L.; Maykuth, P.; Matthesen, G.; Mills, P.C.; Waran, N.; Harris, P.
	Title	Recovery from transport and acclimatisation of competition horses in a hot humid environment			Type	Journal Article
	Year	2001	Publication	Equine Veterinary Journal	Abbreviated Journal	Equine Vet J
	Volume	33	Issue	4	Pages	371-379
	Keywords	Acclimatization/physiology; Animals; Body Temperature; Body Weight; Breeding; Feeding Behavior; Female; Heart Rate; Heat; Heat Stroke/prevention & control/veterinary; Horse Diseases/prevention & control; Horses/physiology; Humidity; Male; Respiration; Sports; *Transportation; Tropical Climate
	Abstract	The aims of the present field-based study were to investigate changes in fit horses undergoing acclimatisation to a hot humid environment and to provide data on which to base recommendations for safe transport and acclimatisation. Six horses (age 7-12 years) were flown from Europe to Atlanta and underwent a 16 day period of acclimatisation. Exercise conditions during acclimatisation (wet bulb globe temperature index 27.6+/-0.0 [mean +/- s.e.]) were more thermally stressful compared with the European climate from which the horses had come (22.0+/-1.8, P<0.001). Following the flight, weight loss was 4.1+/-0.8% bodyweight and took around 7 days to recover. Water intake during the day was significantly increased (P<0.05) compared with night during acclimatisation. Daily mean exercise duration was 72+/-12 min and the majority of work was performed with a heart rate below 120 beats/min. Respiratory rate (fR) was increased (P<0.05) throughout acclimatisation compared with in Europe, but resting morning (AM) and evening (PM) rectal temperature (TREC), heart rate (fC) and plasma volume were unchanged. White blood cell (WBC) count was significantly increased at AM compared with in Europe on Days 4 and 10 of acclimatisation (P<0.01), but was not different by Day 16. In conclusion, horses exposed to hot humid environmental conditions without prior acclimatisation are able to accommodate these stresses and, with appropriate management, remain fit and clinically healthy, without significant risk of heat illness or heat-related disorders, provided they are allowed sufficient time to recover from transport, acclimatisation is undertaken gradually and they are monitored appropriately.
	Address	Centre for Equine Studies, Animal Health Trust, Newmarket, Suffolk, UK
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0425-1644	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:11469770			Approved	no
	Call Number	refbase @ user @			Serial	1917
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	Author	Balakrishnan, G.; Hu, Y.; Spiro, T.G.
	Title	Temperature-jump apparatus with Raman detection based on a solid-state tunable (1.80-2.05 microm) kHz optical parametric oscillator laser			Type	Journal Article
	Year	2006	Publication	Applied Spectroscopy	Abbreviated Journal	Appl Spectrosc
	Volume	60	Issue	4	Pages	347-351
	Keywords	Animals; Cytochromes c/analysis; Horses; Lasers; Myoglobin/metabolism; Spectrum Analysis, Raman/instrumentation/methods; *Temperature
	Abstract	The operating characteristics of a pulsed (10 ns) tunable near-infrared (NIR) laser source are described for temperature-jump (T-jump) applications. A Q-switched Nd:YLF laser (approximately 10 ns pulses) with a 1 kHz repetition rate is used to pump a potassium titanyl arsenate (KTA) crystal-based optical parametric oscillator (OPO), producing approximately 1 mJ NIR pulses that are tunable (1.80-2.05 microm) across the 1.9 microm vibrational overtone band of water. This T-jump source has been coupled to a deep ultraviolet (UV) probe laser for Raman studies of protein dynamics. T-jumps of up to 30 degrees C, as measured via the O-H stretching Raman band of water, are readily achieved. Application to cytochrome c unfolding is demonstrated.
	Address	Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0003-7028	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:16613628			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3764
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	Author	Miksovska, J.; Larsen, R.W.
	Title	Photothermal studies of pH induced unfolding of apomyoglobin			Type	Journal Article
	Year	2003	Publication	Journal of Protein Chemistry	Abbreviated Journal	J Protein Chem
	Volume	22	Issue	4	Pages	387-394
	Keywords	Acoustics; Animals; Apoproteins/chemistry/metabolism; Circular Dichroism; Horses; Myocardium/chemistry; Myoglobin/chemistry/metabolism; Photolysis; Protein Conformation/radiation effects; Protein Denaturation/radiation effects; *Protein Folding; Temperature; Thermodynamics
	Abstract	Conformational dynamic and enthalpy changes associated with pH induced unfolding of apomyoglobin were studied using photoacoustic calorimetry and photothermal beam deflection methods. The transition between the native state and the I intermediate was induced by a nanosecond pH jump from o-nitrobenzaldehyde photolysis. Deconvolution of photoacoustic waves indicates two kinetic processes. The fast phase (T < 50 ns) is characterized by a volume expansion of 8.8 ml mol(-1). This process is followed by a volume contraction of about -22 ml mol(-1) (tau approximately 500 ns). Photothermal beam deflection measurements do not reveal any volume changes on the time scale between approximately 100 micros and 5 ms. We associate the volume contraction with structural changes occurring during the transition between the native state and the I intermediate. The lack of any processes on the ms time scale may indicate the absence of structural events involving larger conformational changes of apomyoglobin after the pH jump.
	Address	Department of Chemistry, University of South Florida, Tampa, Florida 33620, USA
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0277-8033	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:13678303			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3780
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	Author	Hagen, S.J.; Eaton, W.A.
	Title	Two-state expansion and collapse of a polypeptide			Type	Journal Article
	Year	2000	Publication	Journal of Molecular Biology	Abbreviated Journal	J Mol Biol
	Volume	301	Issue	4	Pages	1019-1027
	Keywords	Animals; Computer Simulation; Cytochrome c Group/chemistry/metabolism; Horses; Kinetics; Lasers; Models, Chemical; Peptides/chemistry/metabolism; Protein Conformation; Protein Denaturation; *Protein Folding; Spectrometry, Fluorescence; Temperature; Thermodynamics
	Abstract	The initial phase of folding for many proteins is presumed to be the collapse of the polypeptide chain from expanded to compact, but still denatured, conformations. Theory and simulations suggest that this collapse may be a two-state transition, characterized by barrier-crossing kinetics, while the collapse of homopolymers is continuous and multi-phasic. We have used a laser temperature-jump with fluorescence spectroscopy to measure the complete time-course of the collapse of denatured cytochrome c with nanosecond time resolution. We find the process to be exponential in time and thermally activated, with an apparent activation energy approximately 9 k(B)T (after correction for solvent viscosity). These results indicate that polypeptide collapse is kinetically a two-state transition. Because of the observed free energy barrier, the time scale of polypeptide collapse is dramatically slower than is predicted by Langevin models for homopolymer collapse.
	Address	Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Building 5, Bethesda, MD, 20892-0520, USA
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0022-2836	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:10966803			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3790
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	Author	Shaw, E.B.; Houpt, K.A.; Holmes, D.F.
	Title	Body temperature and behaviour of mares during the last two weeks of pregnancy			Type	Journal Article
	Year	1988	Publication	Equine veterinary journal	Abbreviated Journal	Equine Vet J
	Volume	20	Issue	3	Pages	199-202
	Keywords	Animals; Behavior, Animal; Body Temperature; Circadian Rhythm; Eating; Female; Horses/physiology; Labor, Obstetric/physiology; Motor Activity; Pregnancy; Pregnancy, Animal/*physiology
	Abstract	Average daily core body temperature and behavioural patterns of pregnant mares were studied, in search of definitive signs of parturition within 24 h of the event. Nineteen pony mares were sampled twice daily for core body temperature. A significant temperature drop, averaging 0.1 degrees C (0.2 degrees F) was observed during the day prior to parturition. Between 18.00 h and 06.00 h, during the two weeks before parturition, Thoroughbred and Standardbred mares (n = 52) spent an average 66.8 per cent of their time standing, 27.0 per cent eating, 4.9 per cent lying in sternal recumbency, 1.0 per cent lying in lateral recumbency, and 0.3 per cent walking. On the night before parturition, mares spent significantly less time lying in sternal recumbency than on previous nights and on the night of parturition all behaviour patterns except eating were significantly different from the nights of the two weeks before parturition. There was an increase in walking (5.3 per cent), lying in sternal recumbency (8 per cent) and lying in lateral recumbency (5.3 per cent) whereas standing (53.3 per cent) was decreased. In 58 observed pregnancies, 54 mares (97 per cent) foaled in a recumbent position and 50 mares (86 per cent) foaled between 18.00 h and 06.00 h.
	Address	Department of Physiology, New York State College of Veterinary Medicine, Cornell University, Ithaca 14853
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0425-1644	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:3402416			Approved	no
	Call Number	refbase @ user @			Serial	46
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	Author	Hughes, K.L.; Sulaiman, I.
	Title	The ecology of Rhodococcus equi and physicochemical influences on growth			Type	Journal Article
	Year	1987	Publication	Veterinary Microbiology	Abbreviated Journal	Vet Microbiol
	Volume	14	Issue	3	Pages	241-250
	Keywords	Animals; Feces/microbiology; Horses; Hydrogen-Ion Concentration; Rhodococcus/growth & development; Soil Microbiology; Temperature
	Abstract	Growth of Rhodococcus equi was studied in vitro. Optimal growth occurred under aerobic conditions between pH 7.0 and 8.5, at 30 degrees C. R. equi survived better in a neutral soil (pH 7.3) than it did in two acid soils (pH less than 5.5). It grew substantially better in soils enriched with faeces than in soils alone. Simple organic acids in horse dung, especially acetate and propionate, appear to be important in supporting growth of R. equi in the environment. The ecology of R. equi can be best explained by an environmental cycle allowing its proliferation in dung, influenced by management, grazing behaviour and prevailing climatic conditions. Preventive measures should be aimed at reducing or avoiding focal areas of faecal contamination in the environment.
	Address	School of Veterinary Science, University of Melbourne, Parkville, Vic., Australia
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0378-1135	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:3672866			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	2678
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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
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0006-3495	ISBN		Medium
	Area		Expedition		Conference
	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
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0006-3002	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:1627604			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3800
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	Author	Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K.
	Title	Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide			Type	Journal Article
	Year	1977	Publication	Biochimica et Biophysica Acta	Abbreviated Journal	Biochim Biophys Acta
	Volume	460	Issue	3	Pages	480-489
	Keywords	Animals; Bacteria; Cytochrome c Group; Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics
	Abstract	The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. (Formula: see text.) Thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. The results of this showed that (1) the redox potential of cytochrome c-552, + 0.19 V, is markedly less than that of horse heart cytochrome c. (2) deltaHox of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) deltaSox and deltaSred of cytochrome c-552 are more negative than those of horse heart cytochrome c. (4) kred of cytochrome c-552 is much lower than that of horse heart cytochrome c at room temperature.
	Address
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0006-3002	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:195599			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3815
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