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	Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K.
	Title	Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide			Type	Journal Article
	Year	1977	Publication	Biochimica et Biophysica Acta	Abbreviated Journal	Biochim Biophys Acta
	Volume	460	Issue	3	Pages	480-489
	Keywords	Animals; Bacteria; Cytochrome c Group; Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics
	Abstract	The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. (Formula: see text.) Thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. The results of this showed that (1) the redox potential of cytochrome c-552, + 0.19 V, is markedly less than that of horse heart cytochrome c. (2) deltaHox of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) deltaSox and deltaSred of cytochrome c-552 are more negative than those of horse heart cytochrome c. (4) kred of cytochrome c-552 is much lower than that of horse heart cytochrome c at room temperature.
	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	0006-3002	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:195599			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3815
Permanent link to this record



	Author	Saigo, S.
	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	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.
	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	0006-3002	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:6271238			Approved	no
	Call Number	refbase @ user @			Serial	3871
Permanent link to this record



	Author	Hasumi, H.
	Title	Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method			Type	Journal Article
	Year	1980	Publication	Biochimica et Biophysica Acta	Abbreviated Journal	Biochim Biophys Acta
	Volume	626	Issue	2	Pages	265-276
	Keywords	Circular Dichroism; *Cytochrome c Group; Hydrogen-Ion Concentration; Isomerism; Kinetics; Spectrophotometry
	Abstract	The isomerization of horse-heart ferricytochrome c caused by varying pH was kinetically studied by using circular dichroism (CD) and optical absorption stopped-flow techniques. In the pH range of 7--13, the existence of the three different forms of ferricytochrome c (pH less than 10, pH 10--12, and pH greater than 12) was indicated from the statistical difference CD spectra. On the basis of analyses of the stopped-flow traces in the near-ultraviolet and Soret wavelength regions, the isomerization of ferricytochrome c from neutral form to the above three alkaline forms was interpreted as follows (1) below pH 10, the replacement of the intrinsic ligand of methionine residue by lysine residue occurs; (2) between pH 10 and 12, the uncoupling of the polypeptide chain from close proximity of the heme group occurs first, followed by the interconversion of the intrinsic ligands; and (3) above pH 12, hydroxide form of ferricytochrome c is formed, though the replacement of the intrinsic ligand by extrinsic ligands may occur via different routes from those below pH 12. The CD changes at 288 nm and in the Soret region caused by the pH-jump (down) from pH 6.0 to 1.6 were compared with the appearance of the 620-nm absorption band ascribed to the formation of the high-spin form of ferricytochrome c. Both CD and absorption changes indicated that the isomerization at pH 1.6 consisted of two processes: one proceeded within the dead-time (about 2 ms) of the stopped-flow apparatus and the other proceeded at a determinable rate with the apparatus. On the basis of these results, the isomerization of ferricytochrome c at pH 1.6 was explained as follows: (1) the transition from the low-spin form to the high-spin forms occurs within about 2 ms, the dead-time of the stopped-flow apparatus; and (2) the polypeptide chain is unfolded after the formation of the high-spin form.
	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	0006-3002	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:6260152			Approved	no
	Call Number	refbase @ user @			Serial	3876
Permanent link to this record



	Author	Cho, K.C.; Chan, K.K.
	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	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.
	Address
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language		Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN		ISBN		Medium
	Area		Expedition		Conference
	Notes				Approved	no
	Call Number	refbase @ user @			Serial	3978
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	Gonzalez-Fernandez, J.M.; Atta, S.E.
	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	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	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
Permanent link to this record



	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
Permanent link to this record



	Author	Ryan, C.T.; Schaer, B.L.D.; Nunamaker, D.M.
	Title	A novel wireless data acquisition system for the measurement of hoof accelerations in the exercising horse			Type	Journal Article
	Year	2006	Publication	Equine Veterinary Journal	Abbreviated Journal	Equine Vet J
	Volume	38	Issue	7	Pages	671-674
	Keywords	Acceleration; Animals; Biomechanics; Equipment and Supplies/veterinary; Hoof and Claw/physiology; Horses/physiology; Kinetics; Musculoskeletal Physiology; Physical Conditioning, Animal/*physiology; Running/physiology
	Abstract	REASONS FOR PERFORMING STUDY: A device is needed to safely and wirelessly evaluate accelerations experienced by the horse hoof under a variety of surface conditions with the horse exercising at training or racing speeds. OBJECTIVES: To develop a miniaturised wireless data acquisition system (WDAS) which reliably records hoof accelerations and the times over which they occur in a minimally invasive manner in the exercising Thoroughbred. METHODS: The following criteria were set for device development: production of a lightweight and minimally invasive system, which provides an adequate acceleration range, appropriate frequency response to capture high speed events, and compatibility with a low power wireless telemetry system. Following device development, the WDAS was calibrated, and tested in 6 Thoroughbred horses over a variety of surfaces. RESULTS: Collection of acceleration in seven trials using 6 horses over a variety of surfaces resulted in repeatable acceleration data with respect to the overall characteristic shape of the impact profile. Impact accelerations varied with surface, ranging 34.8-191.7 g. Accelerations on take off were in a similar range, although higher in some trials. Peak impact accelerations tended to larger over the grass paddock surface, than either the indoor arena or the dirt track. During dirt track trials, accelerations on take-off were often comparably larger than those observed on impact within the same footfall. CONCLUSIONS: This study reports the development of a wireless system that successfully measures hoof acceleration in a minimally invasive manner over a variety of surface and exercise conditions. POTENTIAL RELEVANCE: The WDAS will be used in further studies to evaluate various components of the horse-racetrack interface, in an attempt to identify risk factors for musculoskeletal injury in the Thoroughbred racehorse.
	Address	Richard S. Reynolds, Jr. Comparative Orthopedic Research Laboratory, Department of Clinical Studies, New Bolton Center, School of Veterinary Medicine, University of Pennsylvania, Kennett Square, Pennsylvania 19348, 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:17228584			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	4023
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