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	Author	McCutcheon, L.J.; Geor, R.J.
	Title	Influence of training on sweating responses during submaximal exercise in horses			Type	Journal Article
	Year	2000	Publication	Journal of Applied Physiology (Bethesda, Md. : 1985)	Abbreviated Journal	J Appl Physiol
	Volume	89	Issue	6	Pages	2463-2471
	Keywords	Animals; Body Fluids/metabolism; Body Temperature; Body Weight; Environment; Female; Horses/physiology; Ions; Male; Motor Activity/physiology; Oxygen Consumption; Physical Conditioning, Animal/physiology; Sweat/chemistry; Sweating/physiology; Time Factors
	Abstract	Sweating responses were examined in five horses during a standardized exercise test (SET) in hot conditions (32-34 degrees C, 45-55% relative humidity) during 8 wk of exercise training (5 days/wk) in moderate conditions (19-21 degrees C, 45-55% relative humidity). SETs consisting of 7 km at 50% maximal O(2) consumption, determined 1 wk before training day (TD) 0, were completed on a treadmill set at a 6 degrees incline on TD0, 14, 28, 42, and 56. Mean maximal O(2) consumption, measured 2 days before each SET, increased 19% [TD0 to 42: 135 +/- 5 (SE) to 161 +/- 4 ml. kg(-1). min(-1)]. Peak sweating rate (SR) during exercise increased on TD14, 28, 42, and 56 compared with TD0, whereas SRs and sweat losses in recovery decreased by TD28. By TD56, end-exercise rectal and pulmonary artery temperature decreased by 0.9 +/- 0.1 and 1.2 +/- 0.1 degrees C, respectively, and mean change in body mass during the SET decreased by 23% (TD0: 10.1 +/- 0.9; TD56: 7.7 +/- 0.3 kg). Sweat Na(+) concentration during exercise decreased, whereas sweat K(+) concentration increased, and values for Cl(-) concentration in sweat were unchanged. Moderate-intensity training in cool conditions resulted in a 1.6-fold increase in sweating sensitivity evident by 4 wk and a 0.7 +/- 0.1 degrees C decrease in sweating threshold after 8 wk during exercise in hot, dry conditions. Altered sweating responses contributed to improved heat dissipation during exercise and a lower end-exercise core temperature. Despite higher SRs for a given core temperature during exercise, decreases in recovery SRs result in an overall reduction in sweat fluid losses but no change in total sweat ion losses after training.
	Address	Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ontario, Canada N1G 2W1. jmccutch@uoguelph.ca
	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	8750-7587	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:11090603			Approved	no
	Call Number	refbase @ user @			Serial	1922
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	Author	Hrdy, S.B.
	Title	Male-male competition and infanticide among the langurs (Presbytis entellus) of Abu, Rajasthan			Type	Journal Article
	Year	1974	Publication	Folia Primatologica; International Journal of Primatology	Abbreviated Journal	Folia Primatol (Basel)
	Volume	22	Issue	1	Pages	19-58
	Keywords	Aggression; Animals; Animals, Newborn; Coitus; Competitive Behavior; Estrus; Feeding Behavior; Female; Haplorhini; Homing Behavior; Humans; India; Infanticide; Leadership; Male; Maternal Behavior; Population Density; Pregnancy; Rain; Seasons; Sex Factors; Sexual Behavior, Animal; Social Behavior; Temperature; Vocalization, Animal
	Abstract
	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	0015-5713	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:4215710			Approved	no
	Call Number				Serial	2051
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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	Chmel, L.; Hasilikova, A.; Hrasko, J.; Vlacilikova, A.
	Title	The influence of some ecological factors on keratinophilic fungi in the soil			Type	Journal Article
	Year	1972	Publication	Sabouraudia	Abbreviated Journal	Sabouraudia
	Volume	10	Issue	1	Pages	26-34
	Keywords	Animals; Arthrodermataceae/growth & development/isolation & purification/metabolism; Carbohydrates; Czechoslovakia; Ecology; Fungi/growth & development/isolation & purification/metabolism; Hair; Horses; Humic Substances; Humidity; Keratins/metabolism; Microsporum/isolation & purification; Mitosporic Fungi/isolation & purification; Phosphates; Seasons; Soil; Soil Microbiology; Species Specificity; Temperature; Trichophyton/isolation & purification
	Abstract
	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	0036-2174	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:5063162			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	2719
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	Author	Duncan, I.J.H.; Widowski, T.M.; Malleau, A.E.; Lindberg, A.C.; Petherick, J.C.
	Title	External factors and causation of dustbathing in domestic hens			Type	Journal Article
	Year	1998	Publication	Behavioural Processes	Abbreviated Journal	Behav. Process.
	Volume	43	Issue	2	Pages	219-228
	Keywords	Dustbathing; Illumination; Laying hens; Radiant heat; Social facilitation; Temperature
	Abstract	Dustbathing is known to be motivated by complex interactions between internal factors which build up over time and external factors, such as the sight of a dusty substrate. In this study, the effects of other external factors were investigated. Environmental temperature was shown to be important; frequencies of dustbathing were greater when hens were held at 22 than at 10[degree sign]C (P<0.01). In a second experiment, a radiant heat source or a radiant heat+light source, balanced to give the same radiant heat, resulted in more dustbathing behaviour during a 1-h stimulus period than during the same period with no stimulus (P<0.05). Components of dustbathing were increased more by the heat+light stimulus than by the heat stimulus alone (P<0.03). In a third experiment, the amount of dustbathing performed by individual hens in cages with dustbaths was increased by the presence of a group of hens dustbathing in an adjoining pen with a dustbath compared with the amount occurring when the hens were absent from the pen.
	Address
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language		Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN		ISBN		Medium
	Area		Expedition		Conference
	Notes				Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3607
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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	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	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	Gilmanshin, R.; Callender, R.H.; Dyer, R.B.
	Title	The core of apomyoglobin E-form folds at the diffusion limit			Type	Journal Article
	Year	1998	Publication	Nature Structural Biology	Abbreviated Journal	Nat Struct Biol
	Volume	5	Issue	5	Pages	363-365
	Keywords	Animals; Apoproteins/chemistry; Diffusion; Horses; Myoglobin/chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature
	Abstract	The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation.
	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	1072-8368	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:9586997			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3795
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