Equine and Animal Cognition Reference Database -- Query Results

	Equine and Animal Cognition Reference Database Home \| Show All \| Simple Search \| Advanced Search	Login Quick Search: Field: contains: ...
	11-20 of 40 records found matching your query:

Search & Display Options

Select All Deselect All

<< 1 2 3 4 >>

List View

Citations

Details

	Records
	Author	Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W.
	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	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	Touma, C.; Sachser, N.; Mostl, E.; Palme, R.
	Title	Effects of sex and time of day on metabolism and excretion of corticosterone in urine and feces of mice			Type	Journal Article
	Year	2003	Publication	General and Comparative Endocrinology	Abbreviated Journal	Gen Comp Endocrinol
	Volume	130	Issue	3	Pages	267-278
	Keywords	Animals; Chromatography, High Pressure Liquid; Circadian Rhythm/physiology; Corticosterone/metabolism/urine; Feces/*chemistry; Female; Immunoenzyme Techniques; Kinetics; Male; Mice; Mice, Inbred C57BL; Reference Values; Sex Factors; Stress/metabolism; Time Factors; Tritium
	Abstract	Non-invasive techniques to monitor stress hormones in small animals like mice offer several advantages and are highly demanded in laboratory as well as in field research. Since knowledge about the species-specific metabolism and excretion of glucocorticoids is essential to develop such a technique, we conducted radiometabolism studies in mice (Mus musculus f. domesticus, strain C57BL/6J). Each mouse was injected intraperitoneally with 740 kBq of 3H-labelled corticosterone and all voided urine and fecal samples were collected for five days. In a first experiment 16 animals (eight of each sex) received the injection at 9 a.m., while eight mice (four of each sex) were injected at 9 p.m. in a second experiment. In both experiments radioactive metabolites were recovered predominantly in the feces, although males excreted significantly higher proportions via the feces (about 73%) than females (about 53%). Peak radioactivity in the urine was detected within about 2h after injection, while in the feces peak concentrations were observed later (depending on the time of injection: about 10h postinjection in experiment 1 and about 4h postinjection in experiment 2, thus proving an effect of the time of day). The number and relative abundance of fecal [3H]corticosterone metabolites was determined by high performance liquid chromatography (HPLC). The HPLC separations revealed that corticosterone was extensively metabolized mainly to more polar substances. Regarding the types of metabolites formed, significant differences were found between males and females, but not between the experiments. Additionally, the immunoreactivity of these metabolites was assessed by screening the HPLC fractions with four enzyme immunoassays (EIA). However, only a newly established EIA for 5alpha-pregnane-3beta,11beta,21-triol-20-one (measuring corticosterone metabolites with a 5alpha-3beta,11beta-diol structure) detected several peaks of radioactive metabolites with high intensity in both sexes, while the other EIAs showed only minor immunoreactivity. Thus, our study for the first time provides substantial information about metabolism and excretion of corticosterone in urine and feces of mice and is the first demonstrating a significant impact of the animals' sex and the time of day. Based on these data it should be possible to monitor adrenocortical activity non-invasively in this species by measuring fecal corticosterone metabolites with the newly developed EIA. Since mice are extensively used in research world-wide, this could open new perspectives in various fields from ecology to behavioral endocrinology.
	Address	Department of Behavioral Biology, Institute of Neuro and Behavioral Biology, University of Muenster, Badestrasse 9, D-48149 Muenster, Germany. touma@uni-muenster.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	0016-6480	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:12606269			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	4086
Permanent link to this record



	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
Permanent link to this record



	Author	Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W.
	Title	Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique			Type	Journal Article
	Year	2001	Publication	Journal of the American Chemical Society	Abbreviated Journal	J Am Chem Soc
	Volume	123	Issue	27	Pages	6649-6653
	Keywords	Animals; Bacterial Proteins; Cytochrome c Group/chemistry; Guanidine/chemistry; Heme/chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Protein Folding
	Abstract	We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding.
	Address	Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 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	0002-7863	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:11439052			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3788
Permanent link to this record



	Author	Gulotta, M.; Gilmanshin, R.; Buscher, T.C.; Callender, R.H.; Dyer, R.B.
	Title	Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape			Type	Journal Article
	Year	2001	Publication	Biochemistry	Abbreviated Journal	Biochemistry
	Volume	40	Issue	17	Pages	5137-5143
	Keywords	Animals; Apoproteins/chemistry; Computer Simulation; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/chemistry; *Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence/instrumentation/methods; Thermodynamics; Tryptophan/chemistry
	Abstract	An acid-destabilized form of apomyoglobin, the so-called E state, consists of a set of heterogeneous structures that are all characterized by a stable hydrophobic core composed of 30-40 residues at the intersection of the A, G, and H helices of the protein, with little other secondary structure and no other tertiary structure. Relaxation kinetics studies were carried out to characterize the dynamics of core melting and formation in this protein. The unfolding and/or refolding response is induced by a laser-induced temperature jump between the folded and unfolded forms of E, and structural changes are monitored using the infrared amide I' absorbance at 1648-1651 cm(-1) that reports on the formation of solvent-protected, native-like helix in the core and by fluorescence emission changes from apomyoglobin's Trp14, a measure of burial of the indole group of this residue. The fluorescence kinetics data are monoexponential with a relaxation time of 14 micros. However, infrared kinetics data are best fit to a biexponential function with relaxation times of 14 and 59 micros. These relaxation times are very fast, close to the limits placed on folding reactions by diffusion. The 14 micros relaxation time is weakly temperature dependent and thus represents a pathway that is energetically downhill. The appearance of this relaxation time in both the fluorescence and infrared measurements indicates that this folding event proceeds by a concomitant formation of compact secondary and tertiary structures. The 59 micros relaxation time is much more strongly temperature dependent and has no fluorescence counterpart, indicating an activated process with a large energy barrier wherein nonspecific hydrophobic interactions between helix A and the G and H helices cause some helix burial but Trp14 remains solvent exposed. These results are best fit by a multiple-pathway kinetic model when U collapses to form the various folded core structures of E. Thus, the results suggest very robust dynamics for core formation involving multiple folding pathways and provide significant insight into the primary processes of protein folding.
	Address	Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, 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	0006-2960	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:11318635			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3789
Permanent link to this record



	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
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.
	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	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
	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:10620304			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3792
Permanent link to this record



	Author	Pierce, M.M.; Nall, B.T.
	Title	Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization			Type	Journal Article
	Year	2000	Publication	Journal of Molecular Biology	Abbreviated Journal	J Mol Biol
	Volume	298	Issue	5	Pages	955-969
	Keywords	Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/chemistry/genetics/metabolism; Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/metabolism; Histidine/genetics/metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics
	Abstract	The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand.
	Address	Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, 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:10801361			Approved	no
	Call Number	refbase @ user @			Serial	3853
Permanent link to this record



	Author	Matzke, S.M.; Oubre, J.L.; Caranto, G.R.; Gentry, M.K.; Galbicka, G.
	Title	Behavioral and immunological effects of exogenous butyrylcholinesterase in rhesus monkeys			Type	Journal Article
	Year	1999	Publication	Pharmacology, Biochemistry, and Behavior	Abbreviated Journal	Pharmacol Biochem Behav
	Volume	62	Issue	3	Pages	523-530
	Keywords	Animals; Antibody Formation/drug effects; Behavior, Animal/drug effects; Butyrylcholinesterase/immunology/pharmacokinetics/*pharmacology; Cognition/drug effects; Color Perception/drug effects; Conditioning, Operant/drug effects; Discrimination Learning/drug effects; Half-Life; Horses; Humans; Macaca mulatta; Male
	Abstract	Although conventional therapies prevent organophosphate (OP) lethality, laboratory animals exposed to such treatments typically display behavioral incapacitation. Pretreatment with purified exogenous human or equine serum butyrylcholinesterase (Eq-BuChE), conversely, has effectively prevented OP lethality in rats and rhesus monkeys, without producing the adverse side effects associated with conventional treatments. In monkeys, however, using a commercial preparation of Eq-BuChE has been reported to incapacitate responding. In the present study, repeated administration of commercially prepared Eq-BuChE had no systematic effect on behavior in rhesus monkeys as measured by a six-item serial probe recognition task, despite 7- to 18-fold increases in baseline BuChE levels in blood. Antibody production induced by the enzyme was slight after the first injection and more pronounced following the second injection. The lack of behavioral effects, the relatively long in vivo half-life, and the previously demonstrated efficacy of BuChE as a biological scavenger for highly toxic OPs make BuChE potentially more effective than current treatment regimens for OP toxicity.
	Address	Walter Reed Army Institute of Research, Washington, DC 20307-5100, 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	0091-3057	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:10080246			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	4064
Permanent link to this record



	Author	Galloux, P.; Barrey, E.
	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	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
	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		ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:9354287			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3797
Permanent link to this record

Select All Deselect All

<< 1 2 3 4 >>

Details

CQL Search | Library Search | Show Record | Extract Citations

Help