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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 1 Pages (down) 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 Gonzalez-Fernandez, J.M.; Atta, S.E. openurl 
  Title Facilitated transport of oxygen in the presence of membranes in the diffusion path Type Journal Article
  Year 1982 Publication Biophysical Journal Abbreviated Journal Biophys J  
  Volume 38 Issue 2 Pages (down) 133-141  
  Keywords Animals; Biological Transport, Active; Cell Membrane/*metabolism; Diffusion; Dogs; Horses; Humans; Kinetics; Mathematics; *Models, Biological; Muscles/*metabolism; Oxygen/*metabolism  
  Abstract Most of the experimental observations on facilitated transport have been done with millipore filters, and all the theoretical studies have assumed homogeneous spatial properties. In striated muscle there exist membranes that may impede the diffusion of the carrier myoglobin. In this paper a theoretical study is undertaken to analyze the transport in the presence of membranes in the diffusion path. For the numerical computations physiologically relevant values of the parameters were chosen. The numerical results indicate that the presence of membranes tends to decrease the facilitation. For the nonlinear chemical kinetics of the reaction of oxygen with the carrier, this decrement also depends on the location of the membranes. At the higher oxygen concentration side of each membrane the flow of combined oxygen is transferred to the flow of dissolved oxygen. The reverse process occurs at the lower concentration side. Jump discontinuities of the concentration of the oxygen-carrier compound at each membrane are associated with these transfers. The decrement of facilitation is due to the cumulative effect of these jump discontinuities.  
  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 0006-3495 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:7093418 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3806  
Permanent link to this record
 
 
Author Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. doi  openurl
  Title Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods Type Journal Article
  Year 1994 Publication Proteins Abbreviated Journal Proteins  
  Volume 19 Issue 2 Pages (down) 110-119  
  Keywords Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea  
  Abstract The refolding kinetics of horse cyanometmyoglobin induced by concentration jump of urea was investigated by five optical probe stopped-flow methods: absorption at 422 nm, tryptophyl fluorescence at around 340 nm, circular dichroism (CD) at 222 nm, CD at 260 nm, and CD at 422 nm. In the refolding process, we detected three phases with rate constants of > 1 x 10(2) s-1, (4.5-9.3) s-1, and (2-5) x 10(-3) s-1. In the fastest phase, a substantial amount of secondary structure (approximately 40%) is formed within the dead time of the CD stopped-flow apparatus (10.7 ms). The kinetic intermediate populated in the fastest phase is shown to capture a hemindicyanide, suggesting that a “heme pocket precursor” recognized by hemindicyanide must be constructed within the dead time. In the middle phase, most of secondary and tertiary structures, especially around the captured hemindicyanide, have been constructed. In the slowest phase, we detected a minor structural rearrangement accompanying the ligand-exchange reaction in the fifth coordination of ferric iron. We present a possible model for the refolding process of myoglobin in the presence of the heme group.  
  Address Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, 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 0887-3585 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:8090705 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3799  
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 1-2 Pages (down) 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 Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M. openurl 
  Title Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) Type Journal Article
  Year 1979 Publication Journal of Inorganic Biochemistry Abbreviated Journal J Inorg Biochem  
  Volume 11 Issue 2 Pages (down) 95-100  
  Keywords Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism  
  Abstract The electron transfer reactions between Rhus vernicifera stellacyanin and either horse heart cytochrome c or Pseudomonas aeruginosa cytochrome c551 were investigated by rapid reaction techniques. The time course of electron transfer is monophasic under all conditions, and thus consistent with a simple formulation of the reaction. Both stopped-flow and temperature-jump experiments yield equilibrium constants in reasonable agreement with values calculated from the redox potentials. The differences in reaction rate between the two cytochromes and stellacyanin are discussed in terms of the Marcus theory.  
  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 0162-0134 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:228006 Approved no  
  Call Number refbase @ user @ Serial 3879  
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 1 Pages (down) 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  
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  Language English Summary Language Original Title  
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  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 Galloux, P.; Barrey, E. openurl 
  Title Components of the total kinetic moment in jumping horses Type Journal Article
  Year 1997 Publication Equine Veterinary Journal. Supplement Abbreviated Journal Equine Vet J Suppl  
  Volume Issue 23 Pages (down) 41-44  
  Keywords Algorithms; Animals; Exertion/*physiology; Female; Gravitation; Horses/*physiology; Kinetics; Locomotion/*physiology; Male; Models, Biological; Movement/*physiology; Video Recording  
  Abstract Thirty horses were filmed with a panning camera operating at 50 frames/s as they jumped over a 1.20 x 1.20 m fence. The markers of 9 joints on the horse and 7 joints on the rider were tracked in 2D with the TrackEye system. The centre of gravity and moment of inertia of each segment were calculated using a geometric algorithm and a cylindric model, respectively. The kinetic moment of each part of the horse was calculated after filtering, and resampling of data. This method showed the relative contribution of each body segment to the body overall rotation during the take-off, jump and landing phases. It was found that the trunk, hindlimbs and head-neck had the greatest influence. The coordination between the motion of the body segments allowed the horse to control its angular speed of rotation over the fence. This remained nearly constant during the airborne phase (120 +/- 5 degrees/s). During the airborne phase, the kinetic moment was constant because its value was equal to the moment of the external forces (722 +/- 125 kg x m2/s).  
  Address Ecole Nationale d'Equitation, Terrefort, Saumur, France  
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  Notes PMID:9354287 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3797  
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 1 Pages (down) 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.  
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  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 1 Pages (down) 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  
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  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 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 1 Pages (down) 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
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