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Dyson, H.J.; Beattie, J.K. |
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Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
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Journal Article |
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Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
257 |
Issue |
5 |
Pages  |
2267-2273 |
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Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
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Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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English |
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0021-9258 |
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PMID:6277891 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Curtis, S.E.; Stricklin, W.R. |
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Title |
The importance of animal cognition in agricultural animal production systems: an overview |
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Journal Article |
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Year |
1991 |
Publication |
Journal of Animal Science |
Abbreviated Journal |
J. Anim Sci. |
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69 |
Issue |
12 |
Pages |
5001-5007 |
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Keywords |
*Agriculture; Animal Population Groups/*psychology; *Animal Welfare; Animals; *Behavior, Animal; *Cognition; Heat; Helplessness, Learned; Housing, Animal/standards; Immobilization; Nesting Behavior; Pain/psychology/veterinary |
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Abstract |
To describe and then fulfill agricultural animals' needs, we must learn more about their fundamental psychological and behavioral processes. How does this animal feel? Is that animal suffering? Will we ever be able to know these things? Scientists specializing in animal cognition say that there are numerous problems but that they can be overcome. Recognition by scientists of the notion of animal awareness has been increasing in recent years, because of the work of Griffin and others. Feeling, thinking, remembering, and imagining are cognitive processes that are factors in the economic and humane production of agricultural animals. It has been observed that the animal welfare debate depends on two controversial questions: Do animals have subjective feelings? If they do, can we find indicators that reveal them? Here, indirect behavioral analysis approaches must be taken. Moreover, the linear additivity of several stressor effects on a variety of animal traits suggests that some single phenomenon is acting as a “clearinghouse” for many or all of the stresses acting on an animal at any given time, and this phenomenon might be psychological stress. Specific situations animals may encounter in agricultural production settings are discussed with respect to the animals' subjective feelings. |
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University of Illinois, Urbana 61801 |
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0021-8812 |
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PMID:1808193 |
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Equine Behaviour @ team @ |
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2754 |
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Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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Title |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
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Journal Article |
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Year |
2001 |
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Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
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123 |
Issue |
27 |
Pages |
6649-6653 |
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Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
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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. |
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Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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0002-7863 |
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PMID:11439052 |
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Call Number |
Equine Behaviour @ team @ |
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3788 |
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Author |
Tsong, T.Y. |
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Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
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Journal Article |
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Year |
1977 |
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The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
252 |
Issue |
24 |
Pages |
8778-8780 |
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*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
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Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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PMID:200618 |
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refbase @ user @ |
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3882 |
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Author |
Suagee-Bedore, J.K.; Linden, D.R.; Bennett-Wimbush, K. |
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Title |
Effect of Pen Size on Stress Responses of Stall-Housed Horses Receiving One Hour of Daily Turnout |
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Journal Article |
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Year |
2021 |
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Journal of Equine Veterinary Science |
Abbreviated Journal |
J. Equine Vet. Sci. |
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98 |
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103366 |
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Agonistic behaviors; Cortisol; Group turnout; Paddock sizes |
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Abstract |
Group turnout provides important socializing opportunities for horses, particularly those that are primarily stalled. A high percentage of equine injuries occur during group turnout, which could partly be due to the physical constraints of fencing. To investigate appropriate paddock sizes for group turnouts, horses (n = 12) from a single herd were divided into groups of 4, stalled for 24 hours, and then turned out for 1 hour into one of three differently sized pens: 342, 263, and 184 m2 per horse. Groups rotated through pens across 3 days, receiving one treatment per day. Blood was sampled for cortisol concentrations at 08:00 hours each morning, and then at 15 and 60 minutes into the turn out sessions, and 60 minutes after return to individual stalls. Groups rotated through three turnout times: 09:00, 12:00, 14:00 hours. Counts of agonistic behaviors (chasing, contact biting, and kicking) and low-level threats (pinned ears, tail swishing, bite and kick threats) were recorded. When turned out in pens that provided 342 m2 per horse, horses exhibited reduced plasma cortisol concentrations by 15 minutes after turnout and at 1 hour after return to their stalls (P < .05). Horses in pens providing 184 m2 per horse exhibited greater agonistic (P < .001) and low-level threat (P < .01) behaviors than horses in larger pens. These data provide insight into appropriate pen sizes for horses from established herds. Providing at least 342 m2 per horse may reduce the chance of injury in horses accustomed to group turnout. |
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0737-0806 |
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Equine Behaviour @ team @ |
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6694 |
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