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Author Alexander, F.; Collett, R.A. openurl 
  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 (up) 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  
Permanent link to this record
 
 
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 (up) 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  
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  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  
Permanent link to this record
 
 
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 (up) 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  
Permanent link to this record
 
 
Author Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. openurl 
  Title Folding units govern the cytochrome c alkaline transition Type Journal Article
  Year 2003 Publication Journal of Molecular Biology Abbreviated Journal J Mol Biol  
  Volume 331 Issue (up) 1 Pages 37-43  
  Keywords Animals; Cytochrome c Group/*chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; *Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry  
  Abstract The alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways.  
  Address Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.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 0022-2836 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:12875834 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3781  
Permanent link to this record
 
 
Author Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. openurl 
  Title Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump Type Journal Article
  Year 2000 Publication Biophysical Journal Abbreviated Journal Biophys J  
  Volume 78 Issue (up) 1 Pages 405-415  
  Keywords Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence  
  Abstract Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation.  
  Address Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia  
  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 0006-3495 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:10620304 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3792  
Permanent link to this record
 
 
Author Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. openurl 
  Title A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) Type Journal Article
  Year 1977 Publication European Journal of Biochemistry / FEBS Abbreviated Journal Eur J Biochem  
  Volume 77 Issue (up) 1 Pages 193-199  
  Keywords Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature  
  Abstract The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide.  
  Address  
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  Language English Summary Language Original Title  
  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition  
  ISSN 0014-2956 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:20304 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3814  
Permanent link to this record
 
 
Author Bayley, P.; Martin, S.; Anson, M. openurl 
  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 (up) 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  
Permanent link to this record
 
 
Author Saigo, S. openurl 
  Title Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c Type Journal Article
  Year 1981 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta  
  Volume 669 Issue (up) 1 Pages 13-20  
  Keywords Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism  
  Abstract Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization.  
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  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:6271238 Approved no  
  Call Number refbase @ user @ Serial 3871  
Permanent link to this record
 
 
Author Cho, K.C.; Chan, K.K. url  openurl
  Title Kinetics of cold-induced denaturation of metmyoglobin Type Journal Article
  Year 1984 Publication Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology Abbreviated Journal  
  Volume 786 Issue (up) 1-2 Pages 103-108  
  Keywords Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart)  
  Abstract Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order.  
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  Notes Approved no  
  Call Number refbase @ user @ Serial 3978  
Permanent link to this record
 
 
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 (up) 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  
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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 Equine Behaviour @ team @ Serial 3767  
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