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Oliveira-Santos, L.G.R.; Machado-Filho, L.C.P.; Tortato, M.A.; Brusius, L. |
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Title |
Influence of extrinsic variables on activity and habitat selection of lowland tapirs (Tapirus terrestris) in the coastal sand plain shrub, southern Brazil |
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Journal Article |
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Year |
2010 |
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Mammalian Biology – Zeitschrift für Säugetierkunde |
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75 |
Issue  |
3 |
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219-226 |
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Behaviour; Circadian rhythmic; Moonlight; Rainfall; Temperature |
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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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1616-5047 |
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Equine Behaviour @ team @ |
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6140 |
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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)] |
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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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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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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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Admin @ knut @ |
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22 |
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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 |
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Behavioural Processes |
Abbreviated Journal |
Behav. Process. |
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43 |
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2 |
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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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Dunn, M.F.; Branlant, G. |
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Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation |
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Journal Article |
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Year |
1975 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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14 |
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14 |
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3176-3182 |
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*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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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. |
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0006-2960 |
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PMID:238585 |
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Equine Behaviour @ team @ |
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3817 |
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Ballew, R.M.; Sabelko, J.; Gruebele, M. |
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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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Equine Behaviour @ team @ |
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3798 |
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Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. |
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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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1989 |
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Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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996 |
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1-2 |
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49-56 |
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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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Equine Behaviour @ team @ |
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3803 |
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Author |
Cho, K.C.; Chan, K.K. |
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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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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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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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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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22 |
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1 |
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19-58 |
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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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2051 |
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Chmel, L.; Hasilikova, A.; Hrasko, J.; Vlacilikova, A. |
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The influence of some ecological factors on keratinophilic fungi in the soil |
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Journal Article |
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Year |
1972 |
Publication |
Sabouraudia |
Abbreviated Journal |
Sabouraudia |
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10 |
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1 |
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26-34 |
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Animals; Arthrodermataceae/growth & development/isolation & purification/metabolism; Carbohydrates; Czechoslovakia; Ecology; Fungi/growth & development/*isolation & purification/metabolism; Hair; Horses; Humic Substances; Humidity; Keratins/metabolism; Microsporum/isolation & purification; Mitosporic Fungi/isolation & purification; Phosphates; Seasons; Soil; *Soil Microbiology; Species Specificity; Temperature; Trichophyton/isolation & purification |
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0036-2174 |
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PMID:5063162 |
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Equine Behaviour @ team @ |
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2719 |
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Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
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A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
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Journal Article |
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1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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77 |
Issue |
1 |
Pages |
193-199 |
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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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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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Equine Behaviour @ team @ |
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3814 |
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