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Author |
Gill, J. |
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Title |
A new method for continuous recording of motor activity in horses |
Type |
Journal Article |
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Year |
1991 |
Publication |
Comparative Biochemistry and Physiology. A, Comparative Physiology |
Abbreviated Journal  |
Comp Biochem Physiol A |
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Volume |
99 |
Issue |
3 |
Pages |
333-341 |
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Keywords |
Animals; Circadian Rhythm; Female; Horses/*physiology; Monitoring, Physiologic/instrumentation/*veterinary; *Motor Activity; Signal Processing, Computer-Assisted |
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Abstract |
1. The use of an electronic recorder for the horse motor activity was described. 2. Examples of different types of motor activities are given in Figs 1-8. 3. The ultradian pattern of activity in all records was stressed. 4. The possibility of receiving of more physiological informations by this type of apparatus is discussed. |
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Department of Vertebrate Animal Physiology, University of Warsaw, Poland |
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English |
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0300-9629 |
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Notes |
PMID:1678331 |
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no |
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Call Number |
refbase @ user @ |
Serial |
1950 |
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Author |
Piccione, G.; Caola, G.; Refinetti, R. |
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Title |
Temporal relationships of 21 physiological variables in horse and sheep |
Type |
Journal Article |
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Year |
2005 |
Publication |
Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology |
Abbreviated Journal |
Comp Biochem Physiol A Mol Integr Physiol |
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Volume |
142 |
Issue |
4 |
Pages |
389-396 |
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Keywords |
Animals; Behavior, Animal/physiology; Blood Glucose/physiology; Body Temperature/*physiology; Circadian Rhythm/*physiology; Female; Horses/*physiology; Melatonin/blood/*physiology; Motor Activity/*physiology; Rectum/physiology; Sheep/*physiology; Time Factors |
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Abstract |
Daily or circadian oscillation has been documented in a variety of physiological and behavioral processes. Although individual variables have been studied in great detail, very few studies have been conducted on the temporal relationships between the rhythms of different variables. It is not known whether the circadian pacemaker generates each and every rhythm individually or whether most rhythms are simply derived from a few clock-controlled rhythms. As a first step in elucidating this issue, 21 physiological variables were recorded simultaneously in horse and sheep. The results indicated that, in both species, different variables exhibit different degrees of daily rhythmicity and reach their daily peaks at different times of the day. The variables exhibiting strongest rhythmicity were locomotor activity, rectal temperature, and plasma concentrations of melatonin and glucose. Comparison of rhythmicity and acrophase in the various rhythms allowed inferences to be made about mechanisms of causation. |
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Dipartimento di Morfologia, Biochimica, Fisiologia e Produzioni Animali, Facolta di Medicina Veterinaria, Universita degli Studi di Messina, 98168 Messina, Italy |
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English |
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ISSN |
1095-6433 |
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Notes |
PMID:16290083 |
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no |
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Call Number |
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Serial |
1884 |
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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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Language |
French |
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Original Title |
Proprietes spectrales du plasminogene porcin. Etude de la transition acide |
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ISSN |
0014-2956 |
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Notes |
PMID:4326 |
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no |
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Call Number |
Admin @ knut @ |
Serial |
22 |
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Author |
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
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Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
Type |
Journal Article |
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Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
113 |
Issue |
3 |
Pages |
425-433 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism |
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Abstract |
Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion. |
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English |
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ISSN |
0014-2956 |
ISBN |
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Notes |
PMID:7011796 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3810 |
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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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English |
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ISSN |
0014-2956 |
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Notes |
PMID:20304 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
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Author |
Saigo, S. |
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Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
Type |
Journal Article |
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Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
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Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
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Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
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Abstract |
Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH. |
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English |
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ISSN |
0021-924X |
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Notes |
PMID:6270075 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M. |
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Title |
Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) |
Type |
Journal Article |
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Year |
1979 |
Publication |
Journal of Inorganic Biochemistry |
Abbreviated Journal |
J Inorg Biochem |
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Volume |
11 |
Issue |
2 |
Pages |
95-100 |
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Keywords |
Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism |
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Abstract |
The electron transfer reactions between Rhus vernicifera stellacyanin and either horse heart cytochrome c or Pseudomonas aeruginosa cytochrome c551 were investigated by rapid reaction techniques. The time course of electron transfer is monophasic under all conditions, and thus consistent with a simple formulation of the reaction. Both stopped-flow and temperature-jump experiments yield equilibrium constants in reasonable agreement with values calculated from the redox potentials. The differences in reaction rate between the two cytochromes and stellacyanin are discussed in terms of the Marcus theory. |
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English |
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ISSN |
0162-0134 |
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Notes |
PMID:228006 |
Approved |
no |
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Call Number |
refbase @ user @ |
Serial |
3879 |
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Author |
Brown, R.F.; Houpt, K.A.; Schryver, H.F. |
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Title |
Stimulation of food intake in horses by diazepam and promazine |
Type |
Journal Article |
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Year |
1976 |
Publication |
Pharmacology, biochemistry, and behavior |
Abbreviated Journal |
Pharmacol Biochem Behav |
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Volume |
5 |
Issue |
4 |
Pages |
495-497 |
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Keywords |
Age Factors; Animals; Diazepam/*pharmacology; Diet; Feeding Behavior/*drug effects; Female; Horses/*physiology; Male; Promazine/*pharmacology; Stimulation, Chemical |
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Abstract |
In two adult horses doses of 0.02-0.03 mg/kg diazepam, intravenously, increased 1 hr intake 54-75% above control levels. Intake was stimulated when the diet was a high grain, calorically dense one and also when the diet was a high fiber, calorically dilute one. Two young rapidly growing weanling horses showed an even more pronounced stimulation of intake. Following diazepam 1 hr intake was increased 105-240% above control lelvels. Promazine at a dose of 0.5 mg/kg also stimulated intake in adult horses, but not as markedly as did diazepam. A transquilizer and a neuroleptic appear to have a stimulatory eff upon short-term intake in horses. |
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English |
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ISSN |
0091-3057 |
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Notes |
PMID:1005496 |
Approved |
no |
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Call Number |
refbase @ user @ |
Serial |
60 |
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Author |
Matzke, S.M.; Oubre, J.L.; Caranto, G.R.; Gentry, M.K.; Galbicka, G. |
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Title |
Behavioral and immunological effects of exogenous butyrylcholinesterase in rhesus monkeys |
Type |
Journal Article |
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Year |
1999 |
Publication |
Pharmacology, Biochemistry, and Behavior |
Abbreviated Journal |
Pharmacol Biochem Behav |
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Volume |
62 |
Issue |
3 |
Pages |
523-530 |
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Keywords |
Animals; Antibody Formation/drug effects; Behavior, Animal/*drug effects; Butyrylcholinesterase/*immunology/pharmacokinetics/*pharmacology; Cognition/drug effects; Color Perception/drug effects; Conditioning, Operant/drug effects; Discrimination Learning/drug effects; Half-Life; Horses; Humans; Macaca mulatta; Male |
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Abstract |
Although conventional therapies prevent organophosphate (OP) lethality, laboratory animals exposed to such treatments typically display behavioral incapacitation. Pretreatment with purified exogenous human or equine serum butyrylcholinesterase (Eq-BuChE), conversely, has effectively prevented OP lethality in rats and rhesus monkeys, without producing the adverse side effects associated with conventional treatments. In monkeys, however, using a commercial preparation of Eq-BuChE has been reported to incapacitate responding. In the present study, repeated administration of commercially prepared Eq-BuChE had no systematic effect on behavior in rhesus monkeys as measured by a six-item serial probe recognition task, despite 7- to 18-fold increases in baseline BuChE levels in blood. Antibody production induced by the enzyme was slight after the first injection and more pronounced following the second injection. The lack of behavioral effects, the relatively long in vivo half-life, and the previously demonstrated efficacy of BuChE as a biological scavenger for highly toxic OPs make BuChE potentially more effective than current treatment regimens for OP toxicity. |
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Walter Reed Army Institute of Research, Washington, DC 20307-5100, USA |
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0091-3057 |
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Notes |
PMID:10080246 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4064 |
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Author |
Choleris, E.; Kavaliers, M. |
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Title |
Social Learning in Animals: Sex Differences and Neurobiological Analysis |
Type |
Journal Article |
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Year |
1999 |
Publication |
Pharmacology Biochemistry and Behavior |
Abbreviated Journal |
Pharmacol. Biochem. Behav. |
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Volume |
64 |
Issue |
4 |
Pages |
767-776 |
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Keywords |
Observational learning; Social learning; Individual learning; Imitation; Social constraints; Social facilitation; male-female differences; Gender differences |
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Abstract |
Social learning where an “individual's behavior is influenced by observation of, or interaction with, another animal or its products” has been extensively documented in a broad variety of species, including humans. Social learning occurs within the complex framework of an animal's social interactions that are markedly affected by factors such as dominance hierarchies, family bonds, age, and sex of the interacting individuals. Moreover, it is clear that social learning is influenced not only by important sexually dimorphic social constraints but also that it involves attention, motivational, and perceptual mechanisms, all of which exhibit substantial male-female differences. Although sex differences have been demonstrated in a wide range of cognitive and behavioral processes, investigations of male-female differences in social learning and its neurobiological substrates have been largely neglected. As such, sex differences in social learning and its neurobiological substrates merit increased attention. This review briefly considers various aspects of the study of social learning in mammals, and indicates where male-female differences have either been described, neglected and, or could have a potential impact. It also describes the results of neurobiological investigations of social learning and considers the relevance of these findings to other sexually dimorphic cognitive processes. |
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Call Number |
refbase @ user @ |
Serial |
575 |
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