| Records |
| Author |
Oliveira-Santos, L.G.R.; Machado-Filho, L.C.P.; Tortato, M.A.; Brusius, L. |
| Title |
Influence of extrinsic variables on activity and habitat selection of lowland tapirs (Tapirus terrestris) in the coastal sand plain shrub, southern Brazil |
Type |
Journal Article |
| Year |
2010 |
Publication |
Mammalian Biology – Zeitschrift für Säugetierkunde |
Abbreviated Journal |
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| Volume |
75 |
Issue |
3 |
Pages |
219-226 |
| Keywords |
Behaviour; Circadian rhythmic; Moonlight; Rainfall; Temperature |
Abstract  |
The objectives of this research were to: 1. evaluate the circadian activity patterns of lowland tapirs (Tapirus terrestris) throughout the seasons and 2. study the influence of moonlight, temperature and rainfall on the activity patterns and habitat selection of this species, in the coastal sand shrub in southern Brazil. From June 2005 to June 2006, eight tapirs were monitored in a large enclosure containing open and vegetation-covered areas, using four camera traps. Differences in activity patterns within seasons were found. Tapir predominately presented nocturnal-crepuscular activity; however, they differed in the winter, with cathemeral activity patterns. Covered areas were mostly used during periods of extreme temperatures, with less diurnal and more nocturnal activities within these areas, on hotter days. Activity in open areas mainly occurred during periods of intermediate temperatures, both during the day and in the night. Moonlight intensity did not influence nocturnal activities. On days of precipitation of 34 mm or more, there was no record of open-area activities, despite constant activity in covered-area. |
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| ISSN |
1616-5047 |
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no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
6140 |
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| Author |
Balakrishnan, G.; Hu, Y.; Spiro, T.G. |
| Title |
Temperature-jump apparatus with Raman detection based on a solid-state tunable (1.80-2.05 microm) kHz optical parametric oscillator laser |
Type |
Journal Article |
| Year |
2006 |
Publication |
Applied Spectroscopy |
Abbreviated Journal |
Appl Spectrosc |
| Volume |
60 |
Issue |
4 |
Pages |
347-351 |
| Keywords |
Animals; Cytochromes c/analysis; Horses; Lasers; Myoglobin/metabolism; Spectrum Analysis, Raman/*instrumentation/*methods; *Temperature |
| 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. |
| Address |
Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA |
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English |
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0003-7028 |
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| Notes |
PMID:16613628 |
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no |
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Equine Behaviour @ team @ |
Serial |
3764 |
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Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K. |
| 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 |
| Year |
1977 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
| Volume |
460 |
Issue |
3 |
Pages |
480-489 |
| Keywords |
Animals; Bacteria; *Cytochrome c Group; *Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics |
| 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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English |
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0006-3002 |
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| Notes |
PMID:195599 |
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Equine Behaviour @ team @ |
Serial |
3815 |
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| Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
| Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
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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 |
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0027-8424 |
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PMID:8650166 |
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no |
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Equine Behaviour @ team @ |
Serial |
3798 |
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| Author |
Gulotta, M.; Rogatsky, E.; Callender, R.H.; Dyer, R.B. |
| Title |
Primary folding dynamics of sperm whale apomyoglobin: core formation |
Type |
Journal Article |
| Year |
2003 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
| Volume |
84 |
Issue |
3 |
Pages |
1909-1918 |
| Keywords |
Animals; Apoproteins/*chemistry; Crystallography/*methods; Horses; Myocardium/chemistry; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Species Specificity; Structure-Activity Relationship; Temperature; Whales |
| 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. |
| Address |
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA. gulotta@aecom.yu.edu |
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English |
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0006-3495 |
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| Notes |
PMID:12609893 |
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Equine Behaviour @ team @ |
Serial |
3783 |
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| Author |
Cho, K.C.; Chan, K.K. |
| Title |
Kinetics of cold-induced denaturation of metmyoglobin |
Type |
Journal Article |
| Year |
1984 |
Publication |
Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology |
Abbreviated Journal |
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| Volume |
786 |
Issue |
1-2 |
Pages |
103-108 |
| Keywords |
Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart) |
| 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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