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Author Machnik, M.; Hegger, I.; Kietzmann, M.; Thevis, M.; Guddat, S.; Schanzer, W. doi  openurl
  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 (up) Serial 1841  
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Author Hubbell, J.A.E.; Muir, W.W. openurl 
  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  
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  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 (up) 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. openurl 
  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  
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  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 (up) Serial 1901  
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Author Jallon, J.M.; Risler, Y.; Iwatsubo, M. openurl 
  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  
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  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 (up) Admin @ knut @ Serial 21  
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Author Geutjens, C.A.; Clayton, H.M.; Kaiser, L.J. url  doi
openurl 
  Title Forces and pressures beneath the saddle during mounting from the ground and from a raised mounting platform Type Journal Article
  Year 2008 Publication The Veterinary Journal Abbreviated Journal  
  Volume 175 Issue 3 Pages 332-337  
  Keywords Electronic saddle mat; Total force; Peak pressure; Equestrian; Kinetics  
  Abstract The objective was to use an electronic pressure mat to measure and compare forces and pressures of the saddle on a horse's back when riders mounted from the ground and with the aid of a mounting platform. Ten riders mounted a horse three times each from the ground and from a 35 cm high mounting platform in random order. Total force (summation of forces over all 256 sensors) was measured and compared at specific points on the force-time curve. Total force was usually highest as the rider's right leg was swinging upwards and was correlated with rider mass. When normalized to rider mass, total force and peak pressure were significantly higher when mounting from the ground than from a raised platform (P < 0.05). The area of highest pressure was on the right side of the withers in 97% of mounting efforts, confirming the importance of the withers in stabilizing the saddle during mounting.  
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  Notes Approved no  
  Call Number (up) Admin @ knut @ Serial 4344  
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Author Meschan, E.M.; Peham, C.; Schobesberger, H.; Licka, T.F. url  doi
openurl 
  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.  
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  Area Expedition Conference  
  Notes Approved no  
  Call Number (up) Admin @ knut @ Serial 4349  
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Author Sukhomlinov, B.F.; Korobov, V.N.; Gonchar, M.V.; Datsiuk, L.A.; Korzhev, V.A. openurl 
  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 (up) Equine Behaviour @ team @ Serial 2681  
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Author Bykov, S.; Lednev, I.; Ianoul, A.; Mikhonin, A.; Munro, C.; Asher, S.A. doi  openurl
  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  
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  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 (up) Equine Behaviour @ team @ Serial 3767  
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Author Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. openurl 
  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 (up) Equine Behaviour @ team @ Serial 3770  
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Author Hirota, S.; Suzuki, M.; Watanabe, Y. openurl 
  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  
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  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 (up) Equine Behaviour @ team @ Serial 3777  
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