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| Author |
Roberts, J.; Hunter, M.L.; Kacelnik, A. |
| Title |
The ground effect and acoustic communication |
Type |
Journal Article |
| Year |
1981 |
Publication |
Animal Behaviour. |
Abbreviated Journal |
Anim. Behav. |
| Volume |
29 |
Issue |
2 |
Pages |
633-634 |
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Serial |
2123 |
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| Author |
McCall, C.A.; Potter, G.D.; Friend, T.H.; Ingram, R.S. |
| Title |
Learning abilities in yearling horses using the Hebb-Williams closed field maze |
Type |
Journal Article |
| Year |
1981 |
Publication |
J. Anim. Sci. |
Abbreviated Journal |
J. Anim. Sci. |
| Volume |
53 |
Issue |
4 |
Pages |
928-933 |
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Cited By (since 1996): 9; Export Date: 24 October 2008 |
Approved |
no |
| Call Number |
Admin @ knut @ |
Serial |
4613 |
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| Author |
Miller, R. |
| Title |
Male aggression, dominance and breeding behaviour in Red Desert feral horses |
Type |
Journal Article |
| Year |
1981 |
Publication |
Zeitschrift fur Tierpsychologie |
Abbreviated Journal |
Z. Tierpsychol. |
| Volume |
57 |
Issue |
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Pages |
340-201 |
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no |
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Equine Behaviour @ team @ |
Serial |
2374 |
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| Author |
Gillan DJ; Premack D; Woodruff G |
| Title |
Reasoning in the chimpanzee: I. Analogical reasoning |
Type |
Journal Article |
| Year |
1981 |
Publication |
J. Exp. Psychol.: Anim. Behav. Process. |
Abbreviated Journal |
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| Volume |
7 |
Issue |
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Pages |
1 |
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Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3063 |
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| Author |
Heird, J.C.; Lennon, A.M.; Bell, R.W. |
| Title |
Effects of early experience on the learning ability of yearling horses |
Type |
Journal Article |
| Year |
1981 |
Publication |
Journal of Animal Science |
Abbreviated Journal |
J. Anim Sci. |
| Volume |
53 |
Issue |
5 |
Pages |
1204-1209 |
| Keywords |
Animals; Conditioning (Psychology); Female; *Handling (Psychology); Horses/*physiology; *Learning |
| Abstract |
Twenty-four yearling Quarter Horse fillies were divided into three groups (I) very limited handling, (II) intermediate handling and (III) extensive handling. At about 14 months of age, each horse was preconditioned for 2 weeks and then run in a simple place-learning T-maze test in which it had to locate its feed. Thirty trials were run daily for 20 days, with the location of the feed changed each day. To retire from the maze, a horse had to meet the criterion: 11 correct responses in 12 tries, with the last eight being consecutive. Horses in Group II required the fewest trials to reach criterion. These horses also learned more and had the highest percentage of correct responses (P less than .05). Mean trainability tended to predict learning ability; however, trainability and trials to criterion were not significantly correlated. Mean emotionality scores indicated a tendency for horses in the intermediately handled group to be less emotional than those in Group I or III. Results indicated that horses with an intermediate amount of handling scored higher on an intermediate test of learning. All handled horses scored higher on learning tests than those not handled. |
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English |
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| ISSN |
0021-8812 |
ISBN |
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| Notes |
PMID:7319966 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3577 |
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| Author |
Saigo, S. |
| Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
Type |
Journal Article |
| Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
| Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
| Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
| 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 |
Summary Language |
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Edition |
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| ISSN |
0021-924X |
ISBN |
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| Notes |
PMID:6270075 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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| Author |
Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. |
| Title |
Nature of the fast and slow refolding reactions of iron(III) cytochrome c |
Type |
Journal Article |
| Year |
1981 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
| Volume |
20 |
Issue |
6 |
Pages |
1622-1630 |
| Keywords |
Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis |
| Abstract |
The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding. |
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English |
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0006-2960 |
ISBN |
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| Notes |
PMID:6261802 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3809 |
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| Author |
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
| Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
Type |
Journal Article |
| Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
| Volume |
113 |
Issue |
3 |
Pages |
425-433 |
| 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 |
| 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 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3810 |
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| Author |
Clutton-Brock, Juliet. |
| Title |
Domesticated animals from early times |
Type |
Book Whole |
| Year |
1981 |
Publication |
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Univ of Texas Press |
Place of Publication |
Austin |
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ISBN |
9780292715325 |
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Approved |
no |
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Equine Behaviour @ team @ |
Serial |
4088 |
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| Author |
Boice, R. |
| Title |
Behavioral comparability of wild and domesticated rats |
Type |
Journal Article |
| Year |
1981 |
Publication |
Behavior Genetics |
Abbreviated Journal |
Behav Genet |
| Volume |
11 |
Issue |
5 |
Pages |
545-553 |
| Keywords |
Animals; *Behavior, Animal; Female; Genetics, Behavioral; Intelligence; Learning; Male; Rats/*genetics |
| Abstract |
The oft-repeated concern for the lack of behavioral comparability of domestic rats with wild forms of Rattus norvegicus is unfounded. Laboratory rats appear to show the potential for all wild-type behaviors, including the most dramatic social postures. Moreover, domestics are capable of assuming a feral existence without difficulty, one where they readily behave in a fashion indistinguishable from wild rats. The one behavioral difference that is clearly established concerns performance in laboratory learning paradigms. The superiority of domestics in these laboratory tasks speaks more to quieting the concerns of degeneracy theorists than to problems of using domestic Norway rats as subjects representative of their species. |
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English |
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0001-8244 |
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| Notes |
PMID:7325955 |
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no |
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Equine Behaviour @ team @ |
Serial |
4144 |
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