| Records |
| Author |
Permyakov, S.E.; Khokhlova, T.I.; Nazipova, A.A.; Zhadan, A.P.; Morozova-Roche, L.A.; Permyakov, E.A. |
| Title |
Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature “phase diagrams” |
Type |
Journal Article |
| Year |
2006 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
| Volume |
65 |
Issue |
4 |
Pages |
984-998 |
| Keywords |
Animals; Apoproteins/chemistry/metabolism; Binding Sites; Calcium/chemistry/*metabolism; Cattle; Edetic Acid/metabolism; Horses/metabolism; Hydrogen-Ion Concentration; Lactalbumin/chemistry/metabolism; Muramidase/*chemistry/*metabolism; Protein Denaturation; Spectrometry, Fluorescence; *Temperature; Thermodynamics; Tryptophan/chemistry/metabolism |
| Abstract |
The most universal approach to the studies of metal binding properties of single-site metal binding proteins, i.e., construction of a “phase diagram” in coordinates of free metal ion concentration-temperature, has been applied to equine lysozyme (EQL). EQL has one relatively strong calcium binding site and shows two thermal transitions, but only one of them is Ca(2+)-dependent. It has been found that the Ca(2+)-dependent behavior of the low temperature thermal transition (I) of EQL can be adequately described based upon the simplest four-states scheme of metal- and temperature-induced structural changes in a protein. All thermodynamic parameters of this scheme were determined experimentally and used for construction of the EQL phase diagram in the pCa-temperature space. Comparison of the phase diagram with that for alpha-lactalbumin (alpha-LA), a close homologue of lysozyme, allows visualization of the differences in thermodynamic behavior of the two proteins. The thermal stability of apo-EQL (transition I) closely resembles that for apo-alpha-LA (mid-temperature 25 degrees C), while the thermal stabilities of their Ca(2+)-bound forms are almost indistinguishable. The native state of EQL has three orders of magnitude lower affinity for Ca(2+) in comparison with alpha-LA while its thermally unfolded state (after the I transition) has about one order lower (K = 15M(-1)) affinity for calcium. Circular dichroism studies of the apo-lysozyme state after the first thermal transition show that it shares common features with the molten globule state of alpha-LA. |
Address  |
Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow region 142290, Russia |
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English |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
1097-0134 |
ISBN |
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| Notes |
PMID:17022083 |
Approved |
no |
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Serial |
1858 |
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| Author |
Hagen, S.J.; Eaton, W.A. |
| Title |
Two-state expansion and collapse of a polypeptide |
Type |
Journal Article |
| Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
| Volume |
301 |
Issue |
4 |
Pages |
1019-1027 |
| 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 |
| 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. |
| 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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| ISSN |
0022-2836 |
ISBN |
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| Notes |
PMID:10966803 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3790 |
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| Author |
Arnold, W.; Ruf, T.; Kuntz, R. |
| Title |
Seasonal adjustment of energy budget in a large wild mammal, the Przewalski horse (Equus ferus przewalskii) II. Energy expenditure |
Type |
Journal Article |
| Year |
2006 |
Publication |
The Journal of experimental biology |
Abbreviated Journal |
J Exp Biol |
| Volume |
209 |
Issue |
Pt 22 |
Pages |
4566-4573 |
| Keywords |
Animals; Animals, Wild/*physiology; Body Temperature; Body Temperature Regulation; Eating; *Energy Metabolism; Female; Heart Rate; Horses/*physiology; Male; Motor Activity; Pregnancy; Reproduction; *Seasons |
| 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. |
| 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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English |
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Edition |
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| ISSN |
0022-0949 |
ISBN |
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| Notes |
PMID:17079726 |
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no |
| Call Number |
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Serial |
1782 |
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| Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
| Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
Type |
Journal Article |
| 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. |
| Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
| Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
| 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. |
| Address |
School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, USA |
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English |
Summary Language |
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Series Issue |
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Edition |
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| ISSN |
0027-8424 |
ISBN |
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Medium |
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Conference |
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| Notes |
PMID:8650166 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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| Author |
Hughes, K.L.; Sulaiman, I. |
| Title |
The ecology of Rhodococcus equi and physicochemical influences on growth |
Type |
Journal Article |
| Year |
1987 |
Publication |
Veterinary Microbiology |
Abbreviated Journal |
Vet Microbiol |
| Volume |
14 |
Issue |
3 |
Pages |
241-250 |
| Keywords |
Animals; Feces/microbiology; Horses; Hydrogen-Ion Concentration; Rhodococcus/*growth & development; *Soil Microbiology; Temperature |
| Abstract |
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. |
| Address |
School of Veterinary Science, University of Melbourne, Parkville, Vic., Australia |
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English |
Summary Language |
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0378-1135 |
ISBN |
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| Notes |
PMID:3672866 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2678 |
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| Author |
Thiel, D.; Jenni-Eiermann, S.; Palme, R. |
| Title |
Measuring corticosterone metabolites in droppings of capercaillies (Tetrao urogallus) |
Type |
Journal Article |
| Year |
2005 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
| Volume |
1046 |
Issue |
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Pages |
96-108 |
| Keywords |
Adrenocorticotropic Hormone/administration & dosage/analysis/metabolism; Animals; Circadian Rhythm; Corticosterone/administration & dosage/*analysis/*metabolism; Feces/*chemistry; Female; Freezing; Galliformes/*metabolism; Male; Reproducibility of Results; Sex Factors; Temperature; Time Factors; Tritium/diagnostic use |
| Abstract |
The capercaillie (Tetrao urogallus), the largest grouse species in the world, is decreasing in numbers in major parts of its distribution range. Disturbances by human outdoor activities are discussed as a possible reason for this population decline. An indicator for disturbances is the increase of the glucocorticoid corticosterone, a stress hormone, which helps to cope with life-threatening situations. However, repeated disturbances might result in a long-term increase of the basal corticosterone concentration, which can result in detrimental effects like reduced fitness and survival of an animal. To measure corticosterone metabolites (CMs) noninvasively in the droppings of free-living capercaillies, first an enzyme immunoassay (EIA) in captive birds had to be selected and validated. Therefore, the excretion pattern of intravenously injected radiolabeled corticosterone was determined and 3H metabolites were characterized. High-performance liquid chromatography (HPLC) separations of the samples containing peak concentrations revealed that corticosterone was extensively metabolized. The HPLC fractions were tested in several EIAs for glucocorticoid metabolites. The physiological relevance of this method was proved after pharmacological stimulation of the adrenocortical activity. Only the recently established cortisone assay, measuring CMs with a 3,11-dione structure, detected an expressed increase of concentrations following ACTH stimulation. To set up a sampling protocol suited for the field, we examined the influence of various storage conditions and time of day on concentrations of CMs. |
| Address |
Swiss Ornithological Institute, 6204 Sempach, Switzerland. dominik.thiel@vogelwarte.ch |
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English |
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Series Issue |
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Edition |
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| ISSN |
0077-8923 |
ISBN |
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| Notes |
PMID:16055846 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4079 |
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