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Cho, K. C., & Chan, K. K. (1984). Kinetics of cold-induced denaturation of metmyoglobin. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 786(1-2), 103–108.
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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Kihara, H. (1981). Comparison of the redox reactions of various types of cytochrome c with iron hexacyanides. Biochimica et Biophysica Acta (BBA) – Bioenergetics, 634, 93–104.
Abstract: The dynamic behavior of various types of cytochromes c in the redox reaction with iron hexacyanides was studied using a temperature-jump method in order to elucidate the molecular mechanism of the redox reaction of cytochromes with their oxidoreductants. Transmittance after the temperature jump changed through a single exponential decay for all cytochromes investigated. Under a constant concentration of anion, the redox reaction of various types of cytochrome c with iron hexacyanides was analyzed according to the scheme: Ki=kt/k-i (i=1,2,3) where C(III) and C(II) are ferric and ferrous cytochromes, respectively, Fe(III) and Fe(II) are ferri- and ferrocyanides, respectively, C(III) [middle dot] Fe(II) is the ferricytochrome-ferrocyanide complex and C(II) [middle dot] Fe(III) is the ferrocytochrome-ferricyanide complex. When step B is slower than the other two steps A and C, τ-1 can be represented approximately as where the bar over the variables denotes the equilibrium value. In a large excess of ferrocyanide against cytochrome, we can estimate k2, k-2, K1 and K3 independently. In the case of horse cytochrome c at 18[degree sign]C in 0.1 M phosphate buffer at pH 7 with 0.3 M KNO3, the estimated parameters are k2 = 100 +/- 50 s-1, k-2 = (3.5 +/- 1.0) [middle dot] 103 s-1, K1 = 15 +/- 7 M-1 and K3 = (8.5 +/- 1.5) [middle dot] 10-4 M. From the same experiments for seven cytochromes (cytochrome c from horse, tuna, Candida krusei, Saccharomyces oviformis, Rhodospirillum rubrum cytochrome c2, Spirulina platensis cytochrome c-554 and Thermus thermophilus cytochrome c-552), the following results can be deduced. (1) Each parameter defined in the scheme above (k2, k-2, K1, K3) diverged beyond the error range. Above all, k2 values of cytochromes c-554 and c-552 are as large as 1 [middle dot] 104 s-1 and much larger than those for the other cytochromes (to 50 approx. 700 S-1). (2) The variance of k2K1 and k-2/K3 are relatively less than the variances of individual parameters (k2, k-2, K1 and K3), which suggests that the values of k2K1 and k-2/K3 have been conserved during the course of evolution.
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Duncan, I. J. H., Widowski, T. M., Malleau, A. E., Lindberg, A. C., & Petherick, J. C. (1998). External factors and causation of dustbathing in domestic hens. Behav. Process., 43(2), 219–228.
Abstract: 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.
Keywords: Dustbathing; Illumination; Laying hens; Radiant heat; Social facilitation; Temperature
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Fazio, E., Medica, P., Cravana, C., Giacoppo, E., & Ferlazzo, A. (2008). Effect of Short-Distance Road Transport on Thyroid Function, Rectal Temperature, Body Weight and Heart Rate of Stallions. In IESM 2008.
Abstract: Aim of study was to investigate the effects of transport stress on thyroid response, body weight, rectal temperature and heart rate changes in one hundred twenty-six healthy stallions in basal conditions, before and after short road transport. One hundred twenty-six Thoroughbreds and crossbreds stallions with previous travelling experience, aged 4 to 15 yr, were transported by road in a commercial trailer for a period of 3 h (distance <300 km). Blood samples and physiological parameters were collected at 0800 (basal I) and at 1100 (basal II), in each horse“s box, one week before the loading and transport in basal conditions, and one week later, at 0800 immediately before loading (pre-transport), and after 3 h period of transport and unloading, on their arrival at the breeding stations (post-transport), in each new horse”s box, within 30 min. Increases in circulating T3, T4 and fT4 levels (P < 0.01), but not for fT3 levels, were observed after transport, as compared to before loading values, irrespective of different breed. Lower T4 and fT4 levels were observed in basal II (P < 0.01) than basal I and before loading values (pre-transport). After transport Thoroughbreds showed higher fT3 (P < 0.05) and fT4 (P < 0.01) levels than crossbred stallions. No significant differences for T3 and T4 changes were observed. A significant increase in rectal temperature (P < 0.01) and heart rate (P < 0.05) was observed after transport, as compared to before loading values (pre-transport). No differences between basal I, basal II and before loading values (pre-transport) for physiological parameters were observed.
The highest T3, T4 and fT4 levels recorded after short transport seem to suggest a preferential release from the thyroid gland. The results indicate that short road transport stress contributes significantly to thyroid hormone changes, according to different breed, and to the increase in rectal temperature and heart rate. No differences related to different age were observed. |
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Brinkmann, L., Gerken, M., & Riek, A. (2015). Energetic adaptations of Shetland pony mares. In Proceedings of the 3. International Equine Science Meeting.
Abstract: Recent results suggest that wild Northern herbivores exhibit signs of a hypometabolism during times of low ambient temperature and food shortage in order to reduce their energetic needs. However, there are speculations that domestic animals lost the ability to reduce energy expenditure. To examine energetic and behavioural responses 10 Shetland pony mares were exposed to different environmental conditions (summer and winter). During winter ponies were allocated into two groups receiving two different food quantities (60% and 100% of maintenance energy requirement). We measured the field metabolic rate, water turn over, body temperature, locomotor activity, lying time, resting heart rate, body mass and body condition score.
In summer, the field metabolic rate of all ponies (FMR; 63.4±15.0 MJ/day) was considerably higher compared with food restricted and control animals in winter (24.6±7.8 and 15.0±1.1 MJ/day, respectively). Furthermore, during summer, locomotor activity, resting heart rate and total water turnover were significantly elevated (P<0.001) compared with winter. Animals receiving a reduced amount of food (N=5) reduced their FMR by 26% compared with control animals (N=5) to compensate for the decreased energy supply. Furthermore, resting heart rate, body mass and body condition score were lower(29.2±2.7 beats/min, 140±22 kg and 3.0±1.0 points, respectively) than in control animals (36.8±41 beats/min, 165±31 kg, 4.4±0.7 points; P<0.05). While no difference could be found in the observed behaviour, nocturnal hypothermia was elevated in restrictively fed animals. Our results indicate that ponies adapt to different climatic conditions by changing their metabolic rate, behaviour and some physiological parameters. When exposed to energy shortage, ponies, like wild herbivores, exhibited hypometabolism and nocturnal hypothermia. Keywords: Body temperature, Energy expenditure, Food restriction, Hypometabolism, Locomotor activity, Shetland pony |
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Balakrishnan, G., Hu, Y., & Spiro, T. G. (2006). Temperature-jump apparatus with Raman detection based on a solid-state tunable (1.80-2.05 microm) kHz optical parametric oscillator laser. Appl Spectrosc, 60(4), 347–351.
Abstract: The operating characteristics of a pulsed (10 ns) tunable near-infrared (NIR) laser source are described for temperature-jump (T-jump) applications. A Q-switched Nd:YLF laser (approximately 10 ns pulses) with a 1 kHz repetition rate is used to pump a potassium titanyl arsenate (KTA) crystal-based optical parametric oscillator (OPO), producing approximately 1 mJ NIR pulses that are tunable (1.80-2.05 microm) across the 1.9 microm vibrational overtone band of water. This T-jump source has been coupled to a deep ultraviolet (UV) probe laser for Raman studies of protein dynamics. T-jumps of up to 30 degrees C, as measured via the O-H stretching Raman band of water, are readily achieved. Application to cytochrome c unfolding is demonstrated.
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Bayley, P., Martin, S., & Anson, M. (1975). Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution. Biochem Biophys Res Commun, 66(1), 303–308.
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Dunn, M. F., & Branlant, G. (1975). Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation. Biochemistry, 14(14), 3176–3182.
Abstract: 1,4,5,6-Tetrahydronicotinamide adenine dinucleotide (H2NADH) has been investigated as a reduced coenzyme analog in the reaction between trans-4-N,N-dimethylaminocinnamaldehyde (I) (lambdamax 398 nm, epsilonmax 3.15 X 10-4 M-minus 1 cm-minus 1) and the horse liver alcohol dehydrogenase-NADH complex. These equilibrium binding and temperature-jump kinetic studies establish the following. (i) Substitution of H2NADH for NADH limits reaction to the reversible formation of a new chromophoric species, lambdamax 468 nm, epsilonmax 5.8 x 10-4 M-minus 1 cm-minus 1. This chromophore is demonstrated to be structurally analogous to the transient intermediate formed during the reaction of I with the enzyme-NADH complex [Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882]. (ii) The process of intermediate formation with the enzyme-NADH complex is independent of pH over the range 6.13-10.54. Although studies were limited to the pH range 5.98-8.72, a similar pH independence appears to hold for the H2NADH system. (iii) Within the ternary complex, I is bound within van der Waal's contact distance of the coenzyme nicotinamide ring. (iv) Formation of the transient intermediate does not involve covalent modification of coenzyme. Based on these findings, we conclude that zinc ion has a Lewis acid function in facilitating the chemical activation of the aldehyde carbonyl for reduction, and that reduced coenzyme plays a noncovalent effector role in this substrate activating step.
Keywords: *Alcohol Oxidoreductases/metabolism; Aldehydes/*pharmacology; Animals; Binding Sites; Enzyme Activation/drug effects; Horses; Hydrogen-Ion Concentration; Kinetics; Liver/enzymology; *NAD/analogs & derivatives/pharmacology; Oxidation-Reduction; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; *Zinc/pharmacology
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Steinhoff, H. J., Schrader, J., & Schlitter, J. (1992). Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals. Biochim Biophys Acta, 1121(3), 269–278.
Abstract: 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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Steinhoff, H. J., Lieutenant, K., & Redhardt, A. (1989). 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. Biochim Biophys Acta, 996(1-2), 49–56.
Abstract: 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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