| Records |
| Author |
Czerlinski, G.H.; Erickson, J.O.; Theorell, H. |
| Title |
Chemical relaxation studies on the horse liver alcohol dehydrogenase system |
Type |
Journal Article |
| Year |
1979 |
Publication |
Physiological Chemistry and Physics |
Abbreviated Journal |
Physiol Chem Phys |
| Volume |
11 |
Issue |
6 |
Pages |
537-569 |
| Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Buffers; Electron Transport; Ethanol/metabolism; Horses; Hydrogen-Ion Concentration; Liver/*enzymology; Mathematics; NAD/metabolism; Oscillometry; Osmolar Concentration; Temperature; Time Factors |
| Abstract |
Chemical relaxation studies on the system horse liver alcohol dehydrogenase, nicotinamide adenine dinucleotide, and ethanol were conducted observing fluorescence changes between 400 and 500 nm. Temperature-jump experiments were performed at pH 6.5, 7.0, 8.0, and 9.0; concentration-jump experiments at pH 9.0. The reciprocal of the slowest relaxation time was found to be linearly dependent upon the enzyme concentration for relatively low enzyme concentrations, as predicted earlier. Use of the wide pH-range necessitated expression of the four apparent dissociation constants of the catalytic reaction cycle in terms of pH-independent constants. The system was described in terms of only one (or two) catalysis-linked protons not associated with the electron transfer. Protonic steps in a buffered system are in rapid equilibrium, too fast to be measured with the equipment available. Assuming only two of the four bimolecular reaction steps in the four-step cycle are fast compared to the remaining two, six cases may be considered with six expressions for the reciprocal of the slowest relaxation time. Comparison with the experimental data revealed that the bimolecular reaction steps governing the slowest relaxation time change with pH. Above the effective time resolution of the temperature-lump instrument with fluorescence detection (0.1 msec) only one other relaxation time was detectable and only at pH 9. This relaxation time, found to be independent of the concentration of all reactants within experimental error (r = 10 +/- 5 msec), is most likely due to an interconversion among ternary complexes. |
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English |
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| ISSN |
0031-9325 |
ISBN |
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Conference |
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| Notes |
PMID:44918 |
Approved |
no |
Call Number  |
Equine Behaviour @ team @ |
Serial |
3813 |
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| Author |
Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
| Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
Type |
Journal Article |
| Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
| Volume |
77 |
Issue |
1 |
Pages |
193-199 |
| 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 |
| 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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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0014-2956 |
ISBN |
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Conference |
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| Notes |
PMID:20304 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
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| Author |
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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Edition |
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| ISSN |
0006-3002 |
ISBN |
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Conference |
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| Notes |
PMID:195599 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3815 |
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| Author |
Bayley, P.; Martin, S.; Anson, M. |
| Title |
Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution |
Type |
Journal Article |
| Year |
1975 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
| Volume |
66 |
Issue |
1 |
Pages |
303-308 |
| Keywords |
*Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors |
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English |
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Edition |
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| ISSN |
0006-291X |
ISBN |
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| Notes |
PMID:1172440 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3816 |
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| Author |
Agrillo, C.; Dadda, M.; Bisazza, A. |
| Title |
Quantity discrimination in female mosquitofish |
Type |
Journal Article |
| Year |
2007 |
Publication |
Animal cognition |
Abbreviated Journal |
Anim. Cogn. |
| Volume |
10 |
Issue |
1 |
Pages |
63-70 |
| Keywords |
Animals; Cognition; *Cyprinodontiformes; *Discrimination Learning; Female; Male; Mathematics; *Pattern Recognition, Visual |
| Abstract |
The ability in animals to count and represent different numbers of objects has received a great deal of attention in the past few decades. Cumulative evidence from comparative studies on number discriminations report obvious analogies among human babies, non-human primates and birds and are consistent with the hypothesis of two distinct and widespread mechanisms, one for counting small numbers (<4) precisely, and one for quantifying large numbers approximately. We investigated the ability to discriminate among different numerosities, in a distantly related species, the mosquitofish, by using the spontaneous choice of a gravid female to join large groups of females as protection from a sexually harassing male. In one experiment, we found that females were able to discriminate between two shoals with a 1:2 numerosity ratio (2 vs. 4, 4 vs. 8 and 8 vs. 16 fish) but failed to discriminate a 2:3 ratio (8 vs. 12 fish). In the second experiment, we studied the ability to discriminate between shoals that differed by one element; females were able to select the larger shoal when the paired numbers were 2 vs. 3 or 3 vs. 4 but not 4 vs. 5 or 5 vs. 6. Our study indicates that numerical abilities in fish are comparable with those of other non-verbal creatures studied; results are in agreement with the hypothesis of the existence of two distinct systems for quantity discrimination in vertebrates. |
| Address |
Department of General Psychology, University of Padova, via Venezia 8, 35131, Padova, Italy. christian.agrillo@unipd.it |
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English |
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Edition |
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1435-9448 |
ISBN |
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| Notes |
PMID:16868736 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
339 |
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| Author |
Jones, J.E.; Antoniadis, E.; Shettleworth, S.J.; Kamil, A.C. |
| Title |
A comparative study of geometric rule learning by nutcrackers (Nucifraga columbiana), pigeons (Columba livia), and jackdaws (Corvus monedula) |
Type |
Journal Article |
| Year |
2002 |
Publication |
Journal of comparative psychology (Washington, D.C. : 1983) |
Abbreviated Journal |
J Comp Psychol |
| Volume |
116 |
Issue |
4 |
Pages |
350-356 |
| Keywords |
Animals; Behavior, Animal/physiology; Birds; Feeding Behavior/physiology; Learning/*physiology; *Mathematics; Random Allocation; Spatial Behavior/*physiology |
| Abstract |
Three avian species, a seed-caching corvid (Clark's nutcrackers; Nucifraga columbiana), a non-seed-caching corvid (jackdaws; Corvus monedula), and a non-seed-caching columbid (pigeons; Columba livia), were tested for ability to learn to find a goal halfway between 2 landmarks when distance between the landmarks varied during training. All 3 species learned, but jackdaws took much longer than either pigeons or nutcrackers. The nutcrackers searched more accurately than either pigeons or jackdaws. Both nutcrackers and pigeons showed good transfer to novel landmark arrays in which interlandmark distances were novel, but inconclusive results were obtained from jackdaws. Species differences in this spatial task appear quantitative rather than qualitative and are associated with differences in natural history rather than phylogeny. |
| Address |
School of Biological Sciences, University of Nebraska-Lincoln, 68588-0118, USA |
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English |
Summary Language |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0735-7036 |
ISBN |
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Expedition |
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Conference |
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| Notes |
PMID:12539930 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
369 |
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| Author |
Brannon, E.M.; Terrace, H.S. |
| Title |
Ordering of the numerosities 1 to 9 by monkeys |
Type |
Journal Article |
| Year |
1998 |
Publication |
Science (New York, N.Y.) |
Abbreviated Journal |
Science |
| Volume |
282 |
Issue |
5389 |
Pages |
746-749 |
| Keywords |
Animals; *Discrimination (Psychology); Macaca mulatta/*psychology; *Mathematics; *Mental Processes |
| Abstract |
A fundamental question in cognitive science is whether animals can represent numerosity (a property of a stimulus that is defined by the number of discriminable elements it contains) and use numerical representations computationally. Here, it was shown that rhesus monkeys represent the numerosity of visual stimuli and detect their ordinal disparity. Two monkeys were first trained to respond to exemplars of the numerosities 1 to 4 in an ascending numerical order (1 --> 2 --> 3 --> 4). As a control for non-numerical cues, exemplars were varied with respect to size, shape, and color. The monkeys were later tested, without reward, on their ability to order stimulus pairs composed of the novel numerosities 5 to 9. Both monkeys responded in an ascending order to the novel numerosities. These results show that rhesus monkeys represent the numerosities 1 to 9 on an ordinal scale. |
| Address |
Department of Psychology, Columbia University, New York, NY 10027, USA. liz@psych.columbia.edu |
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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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0036-8075 |
ISBN |
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Conference |
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| Notes |
PMID:9784133 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
606 |
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| Author |
Czerlinski, G.H.; Wagner, M.; Erickson, J.O.; Theorell, H. |
| Title |
Chemical relaxation studies on the system liver alcohol dehydrogenase, NADH and imidazole |
Type |
Journal Article |
| Year |
1975 |
Publication |
Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry |
Abbreviated Journal |
Acta Chem Scand B |
| Volume |
29 |
Issue |
8 |
Pages |
797-810 |
| Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Computers; Hydrogen-Ion Concentration; Imidazoles/*metabolism; Kinetics; Liver/enzymology/*metabolism; Mathematics; Models, Chemical; NAD/*metabolism; Time Factors |
| Abstract |
Several years ago, Theorell and Czerlinski conducted experiments on the system of horse liver alcohol dehydrogenase, reduced nicotinamide adenine dinucleotide and imidazole, using the first version of the temperature jump apparatus with detection of changes in fluorescence. These early experiments were repeated with improved instrumentation and confirmed the early experiments in general terms. However, the improved detection system allowed to measure a slight concentration dependence of the relaxation time of around 3 ms. Furthermore, the chemical relaxation time was smaller than the one determined earlier (by factor 2). The data were evaluated much more rigorously than before, allowing an appropriate interpretation of the results. The observed relaxation time is largely due to rate constants in an interconversion of ternary complexes, which are faster than three (of the four) dissociation rate constants, determined previously by Theorell and McKinley-McKee.1,2 This fact contributed to earlier difficulties of finding any concentration dependence. However, the binding of imidazole to the binary enzyme-coenzyme complex can be made to couple kinetically into the interconversion rate of the two ternary complexes. The observed signal derives largely from the ternary complex(es). A substantial fluorescence signal change is associated with the observed relaxation process, suggesting a relocation of the imidazole in reference to the nicotinamide moiety of the bound coenzyme. Nine models are considered with two types of coupling of pre-equilibria (none-all). Quantitative evaluations favor the model with two ternary complexes connected by an interconversion outside the four-step (bimolecular) cycle. The ternary complex outside the cycle has much higher fluorescence yield than the one inside. The interconversion equilibrium is near unity for imidazole. If it would be shifted very much to the side of the “dead-end” complex (as in isobutyramide?!), stimulating action could not take place. |
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English |
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Series Issue |
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Edition |
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| ISSN |
0302-4369 |
ISBN |
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| Notes |
PMID:882 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
3887 |
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