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Author |
Cho, K.C.; Chan, K.K. |
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Title |
Kinetics of cold-induced denaturation of metmyoglobin |
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Journal Article |
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1984 |
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Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology |
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Volume |
786 |
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1-2 |
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103-108 |
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Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart) |
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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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refbase @ user @ |
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3978 |
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Author |
Crowell-Davis, S.L.; Houpt, K.A.; Carnevale, J. |
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Title |
Feeding and drinking behavior of mares and foals with free access to pasture and water |
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Journal Article |
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Year |
1985 |
Publication |
Journal of animal science |
Abbreviated Journal |
J. Anim Sci. |
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60 |
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4 |
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883-889 |
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Keywords |
Animals; *Drinking Behavior; *Feeding Behavior; Female; Horses/*physiology; Male; Poaceae; Seasons; Temperature; Time Factors |
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The feeding and drinking behavior of 11 mares and 15 foals living on pasture with free access to water was recorded during 2,340 15-min focal samples taken over 2 yr. Lactating mares on pasture spent about 70% of the day feeding. Foals began feeding on their first day of life. As they grew older, they spent progressively more time feeding, but still spent only 47 +/- 6% of the time feeding by 21 wk of age. Foals fed primarily during the early morning and evening. While grass formed the major proportion of the diet of both foals and mares, they also ate clay, humus, feces, bark, leaves and twigs. Almost all feeding by foals was done while their mothers were feeding. Movement to water sources was frequently, but not invariably, carried out by an entire herd. Frequency (P = .005) but not duration (P greater than .05) of drinking bouts by mares increased as the temperature increased. Frequency was greatest at 30 to 35 C, at which temperature mares drank once every 1.8 h. Frequency of drinking varied with the time of day (P less than .01), being rarest during the early morning (0500 to 0900 h eastern daylight time) and most frequent during the afternoon (1300 to 1700 h). Drinking by foals was very rare. The youngest age at which a foal was observed to drink was 3 wk, and 8 of 15 foals were never observed to drink before weaning. |
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0021-8812 |
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PMID:3988655 |
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refbase @ user @ |
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54 |
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Hughes, K.L.; Sulaiman, I. |
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Title |
The ecology of Rhodococcus equi and physicochemical influences on growth |
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Journal Article |
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Year |
1987 |
Publication |
Veterinary Microbiology |
Abbreviated Journal |
Vet Microbiol |
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14 |
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3 |
Pages |
241-250 |
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Animals; Feces/microbiology; Horses; Hydrogen-Ion Concentration; Rhodococcus/*growth & development; *Soil Microbiology; Temperature |
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Growth of Rhodococcus equi was studied in vitro. Optimal growth occurred under aerobic conditions between pH 7.0 and 8.5, at 30 degrees C. R. equi survived better in a neutral soil (pH 7.3) than it did in two acid soils (pH less than 5.5). It grew substantially better in soils enriched with faeces than in soils alone. Simple organic acids in horse dung, especially acetate and propionate, appear to be important in supporting growth of R. equi in the environment. The ecology of R. equi can be best explained by an environmental cycle allowing its proliferation in dung, influenced by management, grazing behaviour and prevailing climatic conditions. Preventive measures should be aimed at reducing or avoiding focal areas of faecal contamination in the environment. |
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School of Veterinary Science, University of Melbourne, Parkville, Vic., Australia |
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0378-1135 |
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PMID:3672866 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2678 |
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Author |
Shaw, E.B.; Houpt, K.A.; Holmes, D.F. |
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Title |
Body temperature and behaviour of mares during the last two weeks of pregnancy |
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Journal Article |
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Year |
1988 |
Publication |
Equine veterinary journal |
Abbreviated Journal |
Equine Vet J |
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20 |
Issue |
3 |
Pages |
199-202 |
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Keywords |
Animals; *Behavior, Animal; *Body Temperature; Circadian Rhythm; Eating; Female; Horses/*physiology; Labor, Obstetric/*physiology; Motor Activity; Pregnancy; Pregnancy, Animal/*physiology |
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Average daily core body temperature and behavioural patterns of pregnant mares were studied, in search of definitive signs of parturition within 24 h of the event. Nineteen pony mares were sampled twice daily for core body temperature. A significant temperature drop, averaging 0.1 degrees C (0.2 degrees F) was observed during the day prior to parturition. Between 18.00 h and 06.00 h, during the two weeks before parturition, Thoroughbred and Standardbred mares (n = 52) spent an average 66.8 per cent of their time standing, 27.0 per cent eating, 4.9 per cent lying in sternal recumbency, 1.0 per cent lying in lateral recumbency, and 0.3 per cent walking. On the night before parturition, mares spent significantly less time lying in sternal recumbency than on previous nights and on the night of parturition all behaviour patterns except eating were significantly different from the nights of the two weeks before parturition. There was an increase in walking (5.3 per cent), lying in sternal recumbency (8 per cent) and lying in lateral recumbency (5.3 per cent) whereas standing (53.3 per cent) was decreased. In 58 observed pregnancies, 54 mares (97 per cent) foaled in a recumbent position and 50 mares (86 per cent) foaled between 18.00 h and 06.00 h. |
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Department of Physiology, New York State College of Veterinary Medicine, Cornell University, Ithaca 14853 |
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0425-1644 |
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PMID:3402416 |
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refbase @ user @ |
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46 |
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Author |
Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. |
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Title |
Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements |
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Journal Article |
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Year |
1989 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
996 |
Issue |
1-2 |
Pages |
49-56 |
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Keywords |
Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Hydrogen-Ion Concentration; Methemoglobin/*ultrastructure; Motion; Protein Conformation; Temperature; Thermodynamics; Water |
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Temperature-dependent EPR and temperature-jump measurements have been carried out, in order to examine the high-spin to low-spin transition of aquomethemogobin (pH 6.0). Relaxation rates and equilibrium constants could be determined as a function of temperature. As a reaction mechanism for the high-spin to low-spin transition, the binding of N epsilon of His E7 to the heme iron had been proposed; the same mechanism had been suggested for the ms-effect, found in temperature-jump experiments on aquomethemoglobin. A comparison of the thermodynamic quantities, deduced form the measurements in this paper, gives evidence that indeed the same reaction is investigated in both cases. Our results and most of the findings of earlier studies on the spin-state transitions of aquomethemoglobin, using susceptibility, optical, or EPR measurements, can be explained by the transition of methemoglobin with H2O as ligand (with high-spin state at all temperatures) and methemoglobin with ligand N epsilon of His E7 (with a low-spin ground state). Thermal fluctuations of large amplitude have to be postulated for the reaction to take place, so this reaction may be understood as a probe for the study of protein dynamics. |
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Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G |
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0006-3002 |
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PMID:2544230 |
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no |
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Call Number |
Equine Behaviour @ team @ |
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3803 |
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Author |
Steinhoff, H.J.; Schrader, J.; Schlitter, J. |
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Title |
Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals |
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Journal Article |
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Year |
1992 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
1121 |
Issue |
3 |
Pages |
269-278 |
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Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry |
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Association equilibria and association kinetics of the thiocyanate binding reaction to methemoglobin in single crystals and solution are studied using temperature-jump technique and polarized absorption spectroscopy. Different kinetic constants are found for the reaction in solution and crystal phase for the alpha- and beta-subunits of the methemoglobin tetramer. The reduction of the reactivity of the alpha- and beta-subunits in crystalline phase is 6-fold and 2.4-fold, respectively, compared to the values found in solution. The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals. Our results suggest that crystallization of hemoglobin has little influence on small-scale structural fluctuations which are necessary for ligands to get to the binding sites and large-scale structural motions are suppressed. |
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Institut fur Biophysik, Ruhr-Universitat Bochum, Germany |
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0006-3002 |
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PMID:1627604 |
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no |
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Call Number |
Equine Behaviour @ team @ |
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3800 |
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Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
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Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
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Journal Article |
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Year |
1996 |
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Proceedings of the National Academy of Sciences of the United States of America |
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Proc. Natl. Acad. Sci. U.S.A. |
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93 |
Issue |
12 |
Pages |
5759-5764 |
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Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
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The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse. |
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School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, USA |
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0027-8424 |
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PMID:8650166 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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Author |
Duncan, I.J.H.; Widowski, T.M.; Malleau, A.E.; Lindberg, A.C.; Petherick, J.C. |
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Title |
External factors and causation of dustbathing in domestic hens |
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Journal Article |
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Year |
1998 |
Publication |
Behavioural Processes |
Abbreviated Journal |
Behav. Process. |
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43 |
Issue |
2 |
Pages |
219-228 |
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Dustbathing; Illumination; Laying hens; Radiant heat; Social facilitation; Temperature |
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Dustbathing is known to be motivated by complex interactions between internal factors which build up over time and external factors, such as the sight of a dusty substrate. In this study, the effects of other external factors were investigated. Environmental temperature was shown to be important; frequencies of dustbathing were greater when hens were held at 22 than at 10[degree sign]C (P<0.01). In a second experiment, a radiant heat source or a radiant heat+light source, balanced to give the same radiant heat, resulted in more dustbathing behaviour during a 1-h stimulus period than during the same period with no stimulus (P<0.05). Components of dustbathing were increased more by the heat+light stimulus than by the heat stimulus alone (P<0.03). In a third experiment, the amount of dustbathing performed by individual hens in cages with dustbaths was increased by the presence of a group of hens dustbathing in an adjoining pen with a dustbath compared with the amount occurring when the hens were absent from the pen. |
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Equine Behaviour @ team @ |
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3607 |
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Author |
Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
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Title |
The core of apomyoglobin E-form folds at the diffusion limit |
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Journal Article |
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Year |
1998 |
Publication |
Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
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Volume |
5 |
Issue |
5 |
Pages |
363-365 |
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Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
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The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation. |
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1072-8368 |
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PMID:9586997 |
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Equine Behaviour @ team @ |
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3795 |
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Author |
McCutcheon, L.J.; Geor, R.J. |
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Influence of training on sweating responses during submaximal exercise in horses |
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Journal Article |
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Year |
2000 |
Publication |
Journal of Applied Physiology (Bethesda, Md. : 1985) |
Abbreviated Journal |
J Appl Physiol |
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Volume |
89 |
Issue |
6 |
Pages |
2463-2471 |
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Animals; Body Fluids/metabolism; Body Temperature; Body Weight; Environment; Female; Horses/*physiology; Ions; Male; Motor Activity/*physiology; Oxygen Consumption; Physical Conditioning, Animal/*physiology; Sweat/chemistry; Sweating/*physiology; Time Factors |
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Sweating responses were examined in five horses during a standardized exercise test (SET) in hot conditions (32-34 degrees C, 45-55% relative humidity) during 8 wk of exercise training (5 days/wk) in moderate conditions (19-21 degrees C, 45-55% relative humidity). SETs consisting of 7 km at 50% maximal O(2) consumption, determined 1 wk before training day (TD) 0, were completed on a treadmill set at a 6 degrees incline on TD0, 14, 28, 42, and 56. Mean maximal O(2) consumption, measured 2 days before each SET, increased 19% [TD0 to 42: 135 +/- 5 (SE) to 161 +/- 4 ml. kg(-1). min(-1)]. Peak sweating rate (SR) during exercise increased on TD14, 28, 42, and 56 compared with TD0, whereas SRs and sweat losses in recovery decreased by TD28. By TD56, end-exercise rectal and pulmonary artery temperature decreased by 0.9 +/- 0.1 and 1.2 +/- 0.1 degrees C, respectively, and mean change in body mass during the SET decreased by 23% (TD0: 10.1 +/- 0.9; TD56: 7.7 +/- 0.3 kg). Sweat Na(+) concentration during exercise decreased, whereas sweat K(+) concentration increased, and values for Cl(-) concentration in sweat were unchanged. Moderate-intensity training in cool conditions resulted in a 1.6-fold increase in sweating sensitivity evident by 4 wk and a 0.7 +/- 0.1 degrees C decrease in sweating threshold after 8 wk during exercise in hot, dry conditions. Altered sweating responses contributed to improved heat dissipation during exercise and a lower end-exercise core temperature. Despite higher SRs for a given core temperature during exercise, decreases in recovery SRs result in an overall reduction in sweat fluid losses but no change in total sweat ion losses after training. |
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Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ontario, Canada N1G 2W1. jmccutch@uoguelph.ca |
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8750-7587 |
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PMID:11090603 |
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refbase @ user @ |
Serial |
1922 |
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