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	Author	Jallon, J.M.; Risler, Y.; Iwatsubo, M.
	Title	Beef liver L-Glutamate dehydrogenase mechanism: presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH			Type	Journal Article
	Year	1975	Publication	Biochemical and biophysical research communications	Abbreviated Journal	Biochem Biophys Res Commun
	Volume	67	Issue	4	Pages	1527-1536
	Keywords	Animals; Cattle; Glutamate Dehydrogenase/metabolism; Ketoglutaric Acids; Kinetics; Liver/enzymology; Nadp; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet
	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:1038			Approved	no
	Call Number	Admin @ knut @			Serial	21
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	Author	Guo, G.L.; Moffit, J.S.; Nicol, C.J.; Ward, J.M.; Aleksunes, L.A.; Slitt, A.L.; Kliewer, S.A.; Manautou, J.E.; Gonzalez, F.J.
	Title	Enhanced acetaminophen toxicity by activation of the pregnane X receptor			Type	Journal Article
	Year	2004	Publication	Toxicological sciences : an official journal of the Society of Toxicology	Abbreviated Journal	Toxicol Sci
	Volume	82	Issue	2	Pages	374-380
	Keywords	Acetaminophen/pharmacokinetics/toxicity; Analgesics, Non-Narcotic/pharmacokinetics/toxicity; Animals; Aryl Hydrocarbon Hydroxylases/biosynthesis; Biotransformation; Blotting, Northern; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP3A; Membrane Proteins; Mice; Mice, Knockout; Oxidoreductases, N-Demethylating/biosynthesis; Pregnenolone Carbonitrile/pharmacology; Receptors, Cytoplasmic and Nuclear/drug effects; Receptors, Steroid/drug effects; Sulfhydryl Compounds/metabolism
	Abstract	The pregnane X receptor (PXR) is a ligand-activated transcription factor and member of the nuclear receptor superfamily. Activation of PXR represents an important mechanism for the induction of cytochrome P450 3A (CYP3A) enzymes that can convert acetaminophen (APAP) to its toxic intermediate metabolite, N-acetyl-p-benzoquinone imine (NAPQI). Therefore, it was hypothesized that activation of PXR plays a major role in APAP-induced hepatotoxicity. Pretreatment with the PXR activator, pregnenolone 16alpha-carbonitrile (PCN), markedly enhanced APAP-induced hepatic injury, as revealed by increased serum ALT levels and hepatic centrilobular necrosis, in wild-type but not in PXR-null mice. Further analysis showed that following PCN treatment, PXR-null mice had lower CYP3A11 expression, decreased NAPQI formation, and increased maintenance of hepatic glutathione content compared to wild-type mice. Thus, these results suggest that PXR plays a critical role in APAP-induced hepatic toxicity, probably by inducing CYP3A11 expression and hence increasing bioactivation.
	Address	Laboratory of Metabolism, CCR, NCI, NIH, Bethesda, Maryland 20892, 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	1096-6080	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:15456926			Approved	no
	Call Number	refbase @ user @			Serial	71
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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	Machnik, M.; Hegger, I.; Kietzmann, M.; Thevis, M.; Guddat, S.; Schanzer, W.
	Title	Pharmacokinetics of altrenogest in horses			Type	Journal Article
	Year	2007	Publication	Journal of Veterinary Pharmacology and Therapeutics	Abbreviated Journal	J Vet Pharmacol Ther
	Volume	30	Issue	1	Pages	86-90
	Keywords	Administration, Oral; Animals; Chromatography, Liquid/veterinary; Doping in Sports/prevention & control; Horses/metabolism; Male; Mass Spectrometry/veterinary; Progesterone Congeners/administration & dosage/blood/pharmacokinetics/urine; Reproducibility of Results; Substance Abuse Detection/veterinary; Trenbolone/administration & dosage/*analogs & derivatives/blood/pharmacokinetics/urine
	Abstract	The Federation Equestre Internationale has permitted the use of altrenogest in mares for the control of oestrus. However, altrenogest is also suspicious to misuse in competition horses for its potential anabolic effects and suppression of typical male behaviour, and thus is a controlled drug. To investigate the pharmacokinetics of altrenogest in horses we conducted an elimination study. Five oral doses of 44 mug/kg altrenogest were administered to 10 horses at a dose interval of 24 h. Following administration blood and urine samples were collected at appropriate intervals. Altrenogest concentrations were measured by liquid chromatography-tandem mass spectrometry. The plasma levels of altrenogest reached maximal concentrations of 23-75 ng/mL. Baseline values were achieved within 3 days after the final administration. Urine peak concentrations of total altrenogest ranged from 823 to 3895 ng/mL. Twelve days after the final administration concentrations were below the limit of detection (ca 2 ng/mL).
	Address	Institute of Biochemistry, German Sport University, Cologne, Germany. m.machnik@biochem.dshs-koeln.de
	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	0140-7783	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:17217407			Approved	no
	Call Number				Serial	1841
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	Author	Hubbell, J.A.E.; Muir, W.W.
	Title	Antagonism of detomidine sedation in the horse using intravenous tolazoline or atipamezole			Type	Journal Article
	Year	2006	Publication	Equine Veterinary Journal	Abbreviated Journal	Equine Vet J
	Volume	38	Issue	3	Pages	238-241
	Keywords	Animals; Behavior, Animal/drug effects/physiology; Dose-Response Relationship, Drug; Double-Blind Method; Horses/physiology; Hypnotics and Sedatives/antagonists & inhibitors; Imidazoles/antagonists & inhibitors/pharmacology; Infusions, Intravenous/veterinary; Kinetics; Safety; Tolazoline/*pharmacology; Videotape Recording
	Abstract	REASONS FOR PERFORMING STUDY: The ability to shorten the duration of sedation would potentially improve safety and utility of detomidine. OBJECTIVES: To determine the effects of tolazoline and atipamezole after detomidine sedation. HYPOTHESIS: Administration of tolazoline or atipamezole would not affect detomidine sedation. METHODS: In a randomised, placebo-controlled, double-blind, descriptive study, detomidine (0.02 mg/kg bwt i.v.) was administered to 6 mature horses on 4 separate occasions. Twenty-five mins later, each horse received one of 4 treatments: Group 1 saline (0.9% i.v.) as a placebo control; Group 2 atipamezole (0.05 mg/kg bwt i.v.); Group 3 atipamezole (0.1 mg/kg bwt i.v.); and Group 4 tolazoline (4.0 mg/kg bwt i.v.). Sedation, muscle relaxation and ataxia were scored by 3 independent observers at 9 time points. Horses were led through an obstacle course at 7 time points. Course completion time was recorded and the ability of the horse to traverse the course was scored by 3 independent observers. Horses were videotaped before, during and after each trip through the obstacle course. RESULTS: Atipamezole and tolazoline administration incompletely antagonised the effects of detomidine, but the time course to recovery was shortened. CONCLUSIONS AND POTENTIAL RELEVANCE: Single bolus administration of atipamezole or tolazoline produced partial reversal of detomidine sedation and may be useful for minimising detomidine sedation.
	Address	Department of Veterinary Clinical Sciences, College of Veterinary Medicine, Ohio State University, 601 Tharp Street, Columbus, Ohio 43210, 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	0425-1644	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:16706278			Approved	no
	Call Number				Serial	1869
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	Author	Dirikolu, L.; Lehner, A.F.; Karpiesiuk, W.; Hughes, C.; Woods, W.E.; Boyles, J.; Harkins, J.D.; Troppmann, A.; Tobin, T.
	Title	Detection, quantification, metabolism, and behavioral effects of selegiline in horses			Type	Journal Article
	Year	2003	Publication	Veterinary Therapeutics : Research in Applied Veterinary Medicine	Abbreviated Journal	Vet Ther
	Volume	4	Issue	3	Pages	257-268
	Keywords	Administration, Oral; Animals; Behavior, Animal/drug effects; Female; Horses/metabolism; Mass Spectrometry/veterinary; Monoamine Oxidase Inhibitors/administration & dosage/blood/pharmacokinetics/pharmacology/urine; Selegiline/administration & dosage/blood/*pharmacokinetics/pharmacology/urine; Substance Abuse Detection/veterinary
	Abstract	Selegiline ([R]-[-]N,alpha-dimethyl-N-2- propynylphenethylamine or l-deprenyl), an irreversible inhibitor of monoamine oxidase, is a classic antidyskinetic and antiparkinsonian agent widely used in human medicine both as monotherapy and as an adjunct to levodopa therapy. Selegiline is classified by the Association of Racing Commissioners International (ARCI) as a class 2 agent, and is considered to have high abuse potential in racing horses. A highly sensitive LC/MS/MS quantitative analytical method has been developed for selegiline and its potential metabolites amphetamine and methamphetamine using commercially available deuterated analogs of these compounds as internal standards. After administering 40 mg of selegiline orally to two horses, relatively low (<60 ng/ml) concentrations of parent selegiline, amphetamine, and methamphetamine were recovered in urine samples. However, relatively high urinary concentrations of another selegiline metabolite were found, tentatively identified as N- desmethylselegiline. This metabolite was synthesized and found to be indistinguishable from the new metabolite recovered from horse urine, thereby confirming the chemical identity of the equine metabolite. Additionally, analysis of urine samples from four horses dosed with 50 mg of selegiline confirmed that N-desmethylselegiline is the major urinary metabolite of selegiline in horses. In related behavior studies, p.o. and i.v. administration of 30 mg of selegiline produced no significant changes in either locomotor activities or heart rates.
	Address	Department of Biomedical Sciences, College of Veterinary Medicine, Nursing and Allied Health, Tuskegee University, Tuskegee, AL 36088, 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:15136987			Approved	no
	Call Number				Serial	1901
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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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	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	Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R.
	Title	Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c			Type	Journal Article
	Year	2004	Publication	The Protein Journal	Abbreviated Journal	Protein J
	Volume	23	Issue	8	Pages	519-527
	Keywords	Animals; Cytochromes c/chemistry; Enzyme Activation; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry
	Abstract	We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal.
	Address	Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 7/A 43100 Parma, Italy
	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	1572-3887	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:15648974			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3770
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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
	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:14733927			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3777
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