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	Author	Alexander, F.; Collett, R.A.
	Title	Proceedings: Some observations on the pharmacokinetics of trimethoprim in the horse			Type	Journal Article
	Year	1974	Publication	British journal of pharmacology	Abbreviated Journal	Br J Pharmacol
	Volume	52	Issue	1	Pages	142p
	Keywords	Animals; Half-Life; Horses/metabolism; Kinetics; Trimethoprim/metabolism
	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	0007-1188	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:4451793			Approved	no
	Call Number	refbase @ user @			Serial	112
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	Author	Dunn, M.F.; Branlant, G.
	Title	Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation			Type	Journal Article
	Year	1975	Publication	Biochemistry	Abbreviated Journal	Biochemistry
	Volume	14	Issue	14	Pages	3176-3182
	Keywords	Alcohol Oxidoreductases/metabolism; Aldehydes/pharmacology; Animals; Binding Sites; Enzyme Activation/drug effects; Horses; Hydrogen-Ion Concentration; Kinetics; Liver/enzymology; NAD/analogs & derivatives/pharmacology; Oxidation-Reduction; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Zinc/pharmacology
	Abstract	1,4,5,6-Tetrahydronicotinamide adenine dinucleotide (H2NADH) has been investigated as a reduced coenzyme analog in the reaction between trans-4-N,N-dimethylaminocinnamaldehyde (I) (lambdamax 398 nm, epsilonmax 3.15 X 10-4 M-minus 1 cm-minus 1) and the horse liver alcohol dehydrogenase-NADH complex. These equilibrium binding and temperature-jump kinetic studies establish the following. (i) Substitution of H2NADH for NADH limits reaction to the reversible formation of a new chromophoric species, lambdamax 468 nm, epsilonmax 5.8 x 10-4 M-minus 1 cm-minus 1. This chromophore is demonstrated to be structurally analogous to the transient intermediate formed during the reaction of I with the enzyme-NADH complex [Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882]. (ii) The process of intermediate formation with the enzyme-NADH complex is independent of pH over the range 6.13-10.54. Although studies were limited to the pH range 5.98-8.72, a similar pH independence appears to hold for the H2NADH system. (iii) Within the ternary complex, I is bound within van der Waal's contact distance of the coenzyme nicotinamide ring. (iv) Formation of the transient intermediate does not involve covalent modification of coenzyme. Based on these findings, we conclude that zinc ion has a Lewis acid function in facilitating the chemical activation of the aldehyde carbonyl for reduction, and that reduced coenzyme plays a noncovalent effector role in this substrate activating step.
	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	0006-2960	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:238585			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3817
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	Author	Dyson, H.J.; Beattie, J.K.
	Title	Spin state and unfolding equilibria of ferricytochrome c in acidic solutions			Type	Journal Article
	Year	1982	Publication	The Journal of Biological Chemistry	Abbreviated Journal	J Biol Chem
	Volume	257	Issue	5	Pages	2267-2273
	Keywords	Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature
	Abstract	Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions.
	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	0021-9258	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:6277891			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3807
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	Author	Bykov, S.; Lednev, I.; Ianoul, A.; Mikhonin, A.; Munro, C.; Asher, S.A.
	Title	Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region			Type	Journal Article
	Year	2005	Publication	Applied Spectroscopy	Abbreviated Journal	Appl Spectrosc
	Volume	59	Issue	12	Pages	1541-1552
	Keywords	Animals; Equipment Design; Equipment Failure Analysis; Horses; Kinetics; Metmyoglobin/analysis; Myocardium/metabolism; Reproducibility of Results; Sensitivity and Specificity; Spectrophotometry, Ultraviolet/instrumentation/methods; Spectrum Analysis, Raman/instrumentation/methods
	Abstract	We describe a state-of-the-art tunable ultraviolet (UV) Raman spectrometer for the 193-270 nm spectral region. This instrument allows for steady-state and transient UV Raman measurements. We utilize a 5 kHz Ti-sapphire continuously tunable laser (approximately 20 ns pulse width) between 193 nm and 240 nm for steady-state measurements. For transient Raman measurements we utilize one Coherent Infinity YAG laser to generate nanosecond infrared (IR) pump laser pulses to generate a temperature jump (T-jump) and a second Coherent Infinity YAG laser that is frequency tripled and Raman shifted into the deep UV (204 nm) for transient UV Raman excitation. Numerous other UV excitation frequencies can be utilized for selective excitation of chromophoric groups for transient Raman measurements. We constructed a subtractive dispersion double monochromator to minimize stray light. We utilize a new charge-coupled device (CCD) camera that responds efficiently to UV light, as opposed to the previous CCD and photodiode detectors, which required intensifiers for detecting UV light. For the T-jump measurements we use a second camera to simultaneously acquire the Raman spectra of the water stretching bands (2500-4000 cm(-1)) whose band-shape and frequency report the sample temperature.
	Address	Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, 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:16390595			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3767
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	Author	Bayley, P.; Martin, S.; Anson, M.
	Title	Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution			Type	Journal Article
	Year	1975	Publication	Biochemical and Biophysical Research Communications	Abbreviated Journal	Biochem Biophys Res Commun
	Volume	66	Issue	1	Pages	303-308
	Keywords	*Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors
	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	0006-291X	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:1172440			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3816
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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	Meschan, E.M.; Peham, C.; Schobesberger, H.; Licka, T.F.
	Title	The influence of the width of the saddle tree on the forces and the pressure distribution under the saddle			Type	Journal Article
	Year	2007	Publication	The Veterinary Journal	Abbreviated Journal
	Volume	173	Issue	3	Pages	578-584
	Keywords	Saddle fit; Kinematics; Kinetics; Pressure; Saddletree
	Abstract	As there is no statistical evidence that saddle fit influences the load exerted on a horse's back this study was performed to assess the hypothesis that the width of the tree significantly alters the pressure distribution on the back beneath the saddle. Nineteen sound horses were ridden at walk and trot on a treadmill with three saddles differing only in tree width. Kinetic data were recorded by a sensor mat. A minimum of 14 motion cycles were used in each trial. The saddles were classified into four groups depending on fit. For each horse, the saddle with the lowest overall force (LOF) was determined. Saddles were classified as “too-narrow” if they were one size (2 cm) narrower than the LOF saddle, and “too-wide” if they were one size (2 cm) wider than the LOF saddle. Saddles two sizes wider than LOF saddles were classified as “very-wide”. In the group of narrow saddles, the pressure in the caudal third (walk 0.63 N/cm2 +/- 0.10; trot 1.08 N/cm2 +/- 0.26) was significantly higher compared to the LOF saddles (walk 0.50 N/cm2 +/- 0.09; trot 0.86 N/cm2 +/- 0.28). In the middle transversal third, the pressure of the wide saddles (walk 0.73 N/cm2 +/- 0.06; trot 1.52 N/cm2 +/- 0.19) and very-wide saddles (walk 0.77 N/cm2 +/- 0.06; trot 1.57 N/cm2 +/- 0.19) was significantly higher compared to LOF saddles (walk 0.65 N/cm2 +/- 0.10/ 0.63 N/cm2 +/- 0.11; trot 1.33 N/cm2 +/- 0.22/1.27 N/cm2 +/- 0.20). This study demonstrates that the load under poorly fitting saddles is distributed over a smaller area than under properly fitting saddles, leading to potentially harmful pressures peaks.
	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	Admin @ knut @			Serial	4349
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	Author	Haruta, N.; Kitagawa, T.
	Title	Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin			Type	Journal Article
	Year	2002	Publication	Biochemistry	Abbreviated Journal	Biochemistry
	Volume	41	Issue	21	Pages	6595-6604
	Keywords	Animals; Apoproteins/chemistry; Circular Dichroism; Holoenzymes/chemistry; Horses; Hydrochloric Acid/chemistry; Hydrogen-Ion Concentration; Imidazoles/chemistry; Kinetics; Models, Molecular; Myoglobin/chemistry; Peptide Fragments/chemistry; Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman/methods; Tryptophan/*chemistry; Ultraviolet Rays; Whales
	Abstract	The 244-nm excited transient UV resonance Raman spectra are observed for the refolding intermediates of horse apomyoglobin (h-apoMb) with a newly constructed mixed flow cell system, and the results are interpreted on the basis of the spectra observed for the equilibrium acid unfolding of the same protein. The dead time of mixing, which was determined with the appearance of UV Raman bands of imidazolium upon mixing of imidazole with acid, was 150 micros under the flow rate that was adopted. The pH-jump experiments of h-apoMb from pH 2.2 to 5.6 conducted with this device demonstrated the presence of three folding intermediates. On the basis of the analysis of W3 and W7 bands of Trp7 and Trp14, the first intermediate, formed before 250 micros, involved incorporation of Trp14 into the alpha-helix from a random coil. The frequency shift of the W3 band of Trp14 observed for this process was reproduced with a model peptide of the A helix when it forms the alpha-helix. In the second intermediate, formed around 1 ms after the start of refolding, the surroundings of both Trp7 and Trp14 were significantly hydrophobic, suggesting the formation of the hydrophobic core. In the third intermediate appearing around 3 ms, the hydrophobicity was relaxed to the same level as that of the pH 4 equilibrium intermediate, which was investigated in detail with the stationary state technique. The change from the third intermediate to the native state needs more time than 40 ms, while the appearance of the native spectrum after the mixing of the same solutions was confirmed separately.
	Address	School of Mathematical and Physical Sciences, The Graduate University for Advanced Studies, Myodaiji, Okazaki 444-8585, Japan
	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	0006-2960	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:12022863			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3785
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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	Sukhomlinov, B.F.; Korobov, V.N.; Gonchar, M.V.; Datsiuk, L.A.; Korzhev, V.A.
	Title	[Comparative analysis of the peroxidase activity of myoglobins in mammals]			Type	Journal Article
	Year	1987	Publication	Zhurnal Evoliutsionnoi Biokhimii i Fiziologii	Abbreviated Journal	Zh Evol Biokhim Fiziol
	Volume	23	Issue	1	Pages	37-41
	Keywords	Amino Acid Sequence; Animals; Ecology; Evolution; Kinetics; Mammals/metabolism; Myoglobin/metabolism; Peroxidases/metabolism
	Abstract	Studies have been made on the peroxidase activity of metmyoglobins in animals from various ecological groups--the horse Equus caballus, cattle Bos taurus, beaver Castor fiber, otter Lutra lutra, mink Mustela vison and dog Canis familiaris. It was found that the level of this activity in diving animals depends on the duration of their diving, whereas in terrestrial species--on the strength of muscular contraction.
	Address
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	Russian	Summary Language		Original Title	Sravnitel'nyi analiz peroksidaznoi aktivnosti mioglobinov u mlekopitaiushchikh
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0044-4529	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:3564776			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	2681
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