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Author |
Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K. |
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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 |
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Year |
1977 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
460 |
Issue |
3 |
Pages |
480-489 |
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Keywords |
Animals; Bacteria; *Cytochrome c Group; *Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics |
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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. |
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0006-3002 |
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PMID:195599 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3815 |
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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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Equine Behaviour @ team @ |
Serial |
3783 |
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Author |
Rodier, F. |
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Title |
[Spectral properties of porcine plasminogen: study of the acidic transition (author's transl)] |
Type |
Journal Article |
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Year |
1976 |
Publication |
European journal of biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
63 |
Issue |
2 |
Pages |
553-562 |
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Keywords |
Animals; Binding Sites; Guanidines; Hydrogen-Ion Concentration; *Plasminogen; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Ultraviolet; Swine; Temperature |
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Abstract |
The acidic transition of porcine plasminogen, prepared by affinity chromatography, was studied by non-destructive methods. These methods are based on the analysis of the behaviour of the tryptophyls under various conditions. The perturbation of the absorption and emission spectra by pH or temperature and the dynamic quenching of the intrinsic fluorescence are used to obtain information on structural changes which affect the environment of these residues. It is shown that by decreasing pH the fluorescence emission spectra are shifted toward the long wavelengths, with a broadening of the fluorescence band. The same effect can be obtained at constant pH by heating the protein solution. In order to analyze these phenomena, it is assumed that the fluorescence intensities at 355 nm and 328 nm reflect the proportion of the tryptophans which are exposed to the solvent, and buried, respectively. The plot of the ratio of the fluorescence intensities at these wavelengths versus pH or temperature leads to a titration curve showing an unmasking of tryptophans. The proportion of exposed tryptophans is measured by the dynamic fluorescence quenching technique and the data analyzed according to Lehrer. The plot of the fraction of exposed tryptophyls versus pH also shows the unmasking of these chromophores. Thermal perturbation of a solution of plaminogen at neutral pH induces a difference absorption spectrum whose amplitudes at the maxima are proportional to the number of exposed aromatic residues. The comparison with a solution of fully denatured plasminogen in 6 M guanidium chloride, where all the tryptophyls are exposed, shows that the percentage of exposure is equal to 59%. This number is significantly higher than the percentage found by the fluorescence quenching technique (20%), indicating that some tryptophyls are located in crevices, exposed to the solvent but not to the iodide. At acidic pH the absorption difference spectra induced by thermal perturbation are not classical, since they show an inversion and a new band between 300 nm and 305 nm. This band is mentioned in the literature as a minor band of tryptophan which appears when this chromophore is located in an asymmetric environment. On plotting the maximum amplitude of these spectra obtained at acidic pH versus temperature, we obtain a curve indicating that two types of antagonistic interactions are involved in the perturbation of the chromophores spectra. The spectrophotometric titration of plasminogen gives classical absorption difference spectra. By plotting the maximum amplitude at 292 nm versus pH, we obtain a titration curve with an apparent pK of 2.9 units. This pK is acidic which respect to the pK value of a normal carboxyl. This low value can be due to a positively charged group in the neighbourhood of a carboxyl, which interacts with one or more chromophores. When the carboxyl becomes protonated, this positively charged group is free and available to perturb the environment of some chromophores... |
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French |
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Original Title |
Proprietes spectrales du plasminogene porcin. Etude de la transition acide |
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0014-2956 |
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PMID:4326 |
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Call Number |
Admin @ knut @ |
Serial |
22 |
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Author |
Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
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Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
Type |
Journal Article |
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Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
77 |
Issue |
1 |
Pages |
193-199 |
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Keywords |
Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature |
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Abstract |
The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide. |
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0014-2956 |
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PMID:20304 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
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Author |
Hrdy, S.B. |
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Title |
Male-male competition and infanticide among the langurs (Presbytis entellus) of Abu, Rajasthan |
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Journal Article |
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Year |
1974 |
Publication |
Folia Primatologica; International Journal of Primatology |
Abbreviated Journal |
Folia Primatol (Basel) |
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Volume |
22 |
Issue |
1 |
Pages |
19-58 |
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Keywords |
Aggression; Animals; Animals, Newborn; Coitus; *Competitive Behavior; Estrus; Feeding Behavior; Female; *Haplorhini; Homing Behavior; Humans; India; Infanticide; Leadership; Male; Maternal Behavior; Population Density; Pregnancy; Rain; Seasons; Sex Factors; Sexual Behavior, Animal; Social Behavior; Temperature; Vocalization, Animal |
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0015-5713 |
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PMID:4215710 |
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no |
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Serial |
2051 |
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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 |
Issue |
4 |
Pages |
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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Abstract |
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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no |
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Call Number |
refbase @ user @ |
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54 |
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Author |
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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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 |
Arnold, W.; Ruf, T.; Kuntz, R. |
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Title |
Seasonal adjustment of energy budget in a large wild mammal, the Przewalski horse (Equus ferus przewalskii) II. Energy expenditure |
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Journal Article |
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Year |
2006 |
Publication |
The Journal of experimental biology |
Abbreviated Journal |
J Exp Biol |
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Volume |
209 |
Issue |
Pt 22 |
Pages |
4566-4573 |
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Keywords |
Animals; Animals, Wild/*physiology; Body Temperature; Body Temperature Regulation; Eating; *Energy Metabolism; Female; Heart Rate; Horses/*physiology; Male; Motor Activity; Pregnancy; Reproduction; *Seasons |
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Abstract |
Many large mammals show pronounced seasonal fluctuations of metabolic rate (MR). It has been argued, based on studies in ruminants, that this variation merely results from different levels of locomotor activity (LA), and heat increment of feeding (HI). However, a recent study in red deer (Cervus elaphus) identified a previously unknown mechanism in ungulates--nocturnal hypometabolism--that contributed significantly to reduced energy expenditure, mainly during late winter. The relative contribution of these different mechanisms to seasonal adjustments of MR is still unknown, however. Therefore, in the study presented here we quantified for the first time the independent contribution of thermoregulation, LA and HI to heart rate (f(H)) as a measure of MR in a free-roaming large ungulate, the Przewalski horse or Takhi (Equus ferus przewalskii Poljakow). f(H) varied periodically throughout the year with a twofold increase from a mean of 44 beats min(-1) during December and January to a spring peak of 89 beats min(-1) at the beginning of May. LA increased from 23% per day during December and January to a mean level of 53% per day during May, and declined again thereafter. Daily mean subcutaneous body temperature (T(s)) declined continuously during winter and reached a nadir at the beginning of April (annual range was 5.8 degrees C), well after the annual low of air temperature and LA. Lower T(s) during winter contributed considerably to the reduction in f(H). In addition to thermoregulation, f(H) was affected by reproduction, LA, HI and unexplained seasonal variation, presumably reflecting to some degree changes in organ mass. The observed phase relations of seasonal changes indicate that energy expenditure was not a consequence of energy uptake but is under endogenous control, preparing the organism well in advance of seasonal energetic demands. |
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Address |
Research Institute of Wildlife Ecology, University of Veterinary Medicine, Vienna, Savoyenstrasse 1, 1160 Vienna, Austria. walter.arnold@vu-wien.ac.at |
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0022-0949 |
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PMID:17079726 |
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Call Number |
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1782 |
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Author |
Hagen, S.J.; Eaton, W.A. |
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Title |
Two-state expansion and collapse of a polypeptide |
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Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
301 |
Issue |
4 |
Pages |
1019-1027 |
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Keywords |
Animals; Computer Simulation; Cytochrome c Group/*chemistry/*metabolism; Horses; Kinetics; Lasers; Models, Chemical; Peptides/*chemistry/*metabolism; Protein Conformation; Protein Denaturation; *Protein Folding; Spectrometry, Fluorescence; Temperature; Thermodynamics |
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Abstract |
The initial phase of folding for many proteins is presumed to be the collapse of the polypeptide chain from expanded to compact, but still denatured, conformations. Theory and simulations suggest that this collapse may be a two-state transition, characterized by barrier-crossing kinetics, while the collapse of homopolymers is continuous and multi-phasic. We have used a laser temperature-jump with fluorescence spectroscopy to measure the complete time-course of the collapse of denatured cytochrome c with nanosecond time resolution. We find the process to be exponential in time and thermally activated, with an apparent activation energy approximately 9 k(B)T (after correction for solvent viscosity). These results indicate that polypeptide collapse is kinetically a two-state transition. Because of the observed free energy barrier, the time scale of polypeptide collapse is dramatically slower than is predicted by Langevin models for homopolymer collapse. |
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Address |
Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Building 5, Bethesda, MD, 20892-0520, USA |
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English |
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0022-2836 |
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PMID:10966803 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3790 |
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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 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
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Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
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Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
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Abstract |
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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Address |
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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Notes |
PMID:8650166 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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