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Author |
Morton, D.B. |
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Title |
Self-consciousness and animal suffering |
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Journal Article |
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Year |
2000 |
Publication |
Biologist (London, England) |
Abbreviated Journal |
Biologist (London) |
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Volume |
47 |
Issue |
2 |
Pages |
77-80 |
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Keywords |
Animal Population Groups/*psychology; Animal Welfare/*standards; Animals; Behavior, Animal; *Consciousness; Dogs; *Ego; Horses/psychology; Pain/psychology/*veterinary; Pan troglodytes/psychology; Parrots; Pongo pygmaeus/psychology; Self Concept |
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Abstract |
Animals with relatively highly developed brains are likely to experience some degree of self-awareness and the ability to think. As well as being interesting in its own right, self-consciousness matters from an ethical point of view, since it can give rise to forms of suffering above and beyond the immediate physical sensations of pain or distress. This article surveys the evidence for animal self-consciousness and its implications for animal welfare. |
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Division of Primary Care, Public and Occupational Health, School of Medicine, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. d.b.morton@bham.ac.uk |
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0006-3347 |
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PMID:11190233 |
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Call Number |
refbase @ user @ |
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618 |
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Author |
Kirkpatrick, J.F.; Vail, R.; Devous, S.; Schwend, S.; Baker, C.B.; Wiesner, L. |
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Title |
Diurnal variation of plasma testosterone in wild stallions |
Type |
Journal Article |
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Year |
1976 |
Publication |
Biology of reproduction |
Abbreviated Journal |
Biol Reprod |
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Volume |
15 |
Issue |
1 |
Pages |
98-101 |
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Keywords |
Animals; *Circadian Rhythm; Horses/*blood; Male; Montana; Sexual Behavior, Animal; Species Specificity; Testosterone/*blood |
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0006-3363 |
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PMID:986195 |
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refbase @ user @ |
Serial |
149 |
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Author |
Gulotta, M.; Rogatsky, E.; Callender, R.H.; Dyer, R.B. |
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Title |
Primary folding dynamics of sperm whale apomyoglobin: core formation |
Type |
Journal Article |
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Year |
2003 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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Volume |
84 |
Issue |
3 |
Pages |
1909-1918 |
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Keywords |
Animals; Apoproteins/*chemistry; Crystallography/*methods; Horses; Myocardium/chemistry; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Species Specificity; Structure-Activity Relationship; Temperature; Whales |
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Abstract |
The structure, thermodynamics, and kinetics of heat-induced unfolding of sperm whale apomyoglobin core formation have been studied. The most rudimentary core is formed at pH(*) 3.0 and up to 60 mM NaCl. Steady state for ultraviolet circular dichroism and fluorescence melting studies indicate that the core in this acid-destabilized state consists of a heterogeneous composition of structures of approximately 26 residues, two-thirds of the number involved for horse heart apomyoglobin under these conditions. Fluorescence temperature-jump relaxation studies show that there is only one process involved in Trp burial. This occurs in 20 micro s for a 7 degrees jump to 52 degrees C, which is close to the limits placed by diffusion on folding reactions. However, infrared temperature jump studies monitoring native helix burial are biexponential with times of 5 micro s and 56 micro s for a similar temperature jump. Both fluorescence and infrared fast phases are energetically favorable but the slow infrared absorbance phase is highly temperature-dependent, indicating a substantial enthalpic barrier for this process. The kinetics are best understood by a multiple-pathway kinetics model. The rapid phases likely represent direct burial of one or both of the Trp residues and parts of the G- and H-helices. We attribute the slow phase to burial and subsequent rearrangement of a misformed core or to a collapse having a high energy barrier wherein both Trps are solvent-exposed. |
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Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA. gulotta@aecom.yu.edu |
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0006-3495 |
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PMID:12609893 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3783 |
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Author |
Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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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 |
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Year |
2000 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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Volume |
78 |
Issue |
1 |
Pages |
405-415 |
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Keywords |
Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence |
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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. |
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Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia |
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0006-3495 |
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Notes |
PMID:10620304 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3792 |
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Author |
Gonzalez-Fernandez, J.M.; Atta, S.E. |
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Title |
Facilitated transport of oxygen in the presence of membranes in the diffusion path |
Type |
Journal Article |
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Year |
1982 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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Volume |
38 |
Issue |
2 |
Pages |
133-141 |
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Keywords |
Animals; Biological Transport, Active; Cell Membrane/*metabolism; Diffusion; Dogs; Horses; Humans; Kinetics; Mathematics; *Models, Biological; Muscles/*metabolism; Oxygen/*metabolism |
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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. |
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0006-3495 |
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Notes |
PMID:7093418 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3806 |
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Author |
Lees, P.; Tavernor, W.D. |
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Title |
Influence of halothane and catecholamines on heart rate and rhythm in the horse |
Type |
Journal Article |
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Year |
1970 |
Publication |
British journal of pharmacology |
Abbreviated Journal |
Br J Pharmacol |
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Volume |
39 |
Issue |
1 |
Pages |
149-159 |
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Keywords |
Anesthesia, Inhalation; Animals; Arrhythmia/*chemically induced; Atropine/pharmacology; Catecholamines/*pharmacology; Consciousness; Epinephrine/administration & dosage; Ethers; Female; Halothane/*pharmacology; Heart Rate/*drug effects; Horses; Hypercapnia/physiopathology; Isoproterenol/pharmacology; Male; Norepinephrine/pharmacology; Propranolol/pharmacology |
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0007-1188 |
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PMID:5420092 |
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refbase @ user @ |
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103 |
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Author |
Alexander, F. |
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Title |
The effect of diuretics on the faecal excretion of water and electrolytes in horses |
Type |
Journal Article |
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Year |
1977 |
Publication |
British journal of pharmacology |
Abbreviated Journal |
Br J Pharmacol |
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Volume |
60 |
Issue |
4 |
Pages |
589-593 |
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Keywords |
Animals; Body Water/*metabolism; Chlorides/metabolism; Electrolytes/*metabolism; Feces/*analysis; Furosemide/*pharmacology; Horses; Hydrochlorothiazide/*pharmacology; Male; Potassium/metabolism; Sodium/metabolism; Time Factors |
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1. The effect on plasma, urinary and faecal electrolytes of frusemide and hydrochlorthiazide was measured in ponies, mean weight 180 kg. 2. The rapid loss in urine of large quantities of sodium had only a small effect on plasma sodium concentration. 3. Faecal sodium excretion was increased substantially after the administration of frusemide. 4. Frusemide increased faecal potassium during the 48 h following administration and faecal water in the 24/48 h period. It also produced a hypopotassaemia. 5. Hydrochlorthiazide increased faecal chloride during the 24 h after administration. 6. Frusemide increased the intestinal transit time of both liquid (polyethylene glycol) and particulate (Cr2O3) markers. |
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0007-1188 |
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PMID:907872 |
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Call Number |
refbase @ user @ |
Serial |
111 |
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Author |
Alexander, F.; Collett, R.A. |
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Title |
Proceedings: Some observations on the pharmacokinetics of trimethoprim in the horse |
Type |
Journal Article |
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Year |
1974 |
Publication |
British journal of pharmacology |
Abbreviated Journal |
Br J Pharmacol |
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Volume |
52 |
Issue |
1 |
Pages |
142p |
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Keywords |
Animals; Half-Life; Horses/*metabolism; Kinetics; Trimethoprim/*metabolism |
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0007-1188 |
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PMID:4451793 |
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refbase @ user @ |
Serial |
112 |
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Author |
Alexander, F. |
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Title |
Multiple fistulation of the horse's large intestine |
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Journal Article |
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Year |
1970 |
Publication |
The British veterinary journal |
Abbreviated Journal |
Br. Vet. J. |
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Volume |
126 |
Issue |
11 |
Pages |
604-606 |
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Animals; Cecum/physiology; Colon/physiology; Horses/*physiology; Intestinal Fistula; Intestine, Large/*physiology; *Intubation, Gastrointestinal; Methods |
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0007-1935 |
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PMID:5492494 |
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no |
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refbase @ user @ |
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115 |
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Author |
Alexander, F.; Davies, M.E. |
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Title |
Studies on vitamin B12 in the horse |
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Journal Article |
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Year |
1969 |
Publication |
The British veterinary journal |
Abbreviated Journal |
Br. Vet. J. |
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Volume |
125 |
Issue |
4 |
Pages |
169-176 |
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Keywords |
Animals; Biological Assay; Cattle; Chickens; Feces/analysis; Horses/*metabolism; Humans; Lactobacillus/metabolism; Rabbits; Rats; Sheep; Urine/analysis; Vitamin B 12/*analysis |
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0007-1935 |
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PMID:5814055 |
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refbase @ user @ |
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116 |
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