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Author |
Schulman AH; Kaplowitz C |
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Title |
Mirror image response during the first two years of life |
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Year |
1977 |
Publication |
Dev. Psychobiol. |
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10 |
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133 |
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Equine Behaviour @ team @ |
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3039 |
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Author |
Kratzer, D.D.; Netherland, W.M.; Pulse, R.E.; Baker, J.P. |
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Title |
Maze Learning in Quarter Horses |
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Journal Article |
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Year |
1977 |
Publication |
Journal of Animal Science |
Abbreviated Journal |
J. Anim Sci. |
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Volume |
45 |
Issue |
4 |
Pages |
896-902 |
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Abstract |
A two-compartment maze providing a single left- or right-side choice was used to test maze-learning ability in 37 quarter horses. Preference for left- or right-side choices varied among the horses. The taller and thinner horses tended to go left. The horses showed learning ability based on decreases in latency and decreases in errors as trials progressed in a right-side escape pattern. The rate of learning an opposite escape pattern, left-side escape, was faster but owing to the large number of errors occurring when the pattern was reversed, the level of errors did not reduce to a level comparable to that achieved in the right-side escape pattern until adverse stimuli were presented in the blind compartment. Heavier horses took longer to escape from the maze when adverse stimuli were presented. Differences in learning ability for horses fed various levels of dietary protein were not consistent. N1 - |
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Equine Behaviour @ team @ |
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3574 |
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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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0014-2956 |
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PMID:20304 |
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Equine Behaviour @ team @ |
Serial |
3814 |
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Author |
Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K. |
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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 |
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Year |
1977 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
460 |
Issue |
3 |
Pages |
480-489 |
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Keywords |
Animals; Bacteria; *Cytochrome c Group; *Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics |
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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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0006-3002 |
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Notes |
PMID:195599 |
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Call Number |
Equine Behaviour @ team @ |
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3815 |
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Author |
Tsong, T.Y. |
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Title |
Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
Type |
Journal Article |
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Year |
1977 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
252 |
Issue |
24 |
Pages |
8778-8780 |
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*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
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Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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PMID:200618 |
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Call Number |
refbase @ user @ |
Serial |
3882 |
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Author |
Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K.; Oshima, T. |
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Title |
Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide |
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Journal Article |
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Year |
1977 |
Publication |
Biochimica et Biophysica Acta (BBA) – Bioenergetics |
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Volume |
460 |
Issue |
3 |
Pages |
480-489 |
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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. 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) [up triangle, open]Hox++ of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) [up triangle, open]Hox++ and [up triangle, open]Sred++ of cytoochrome 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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refbase @ user @ |
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3986 |
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Author |
Levy, J. |
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Title |
The mammalian brain and the adaptive advantage of cerebral asymmetry |
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Journal Article |
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Year |
1977 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
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Volume |
299 |
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Pages |
264-272 |
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*Adaptation, Physiological; Adaptation, Psychological/physiology; Animals; Behavior, Animal/physiology; Brain/*physiology; Cognition/physiology; Dominance, Cerebral/*physiology; *Evolution; Humans; Intelligence; Perception/physiology |
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0077-8923 |
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PMID:280207 |
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Equine Behaviour @ team @ |
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4137 |
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Author |
Packer, C. |
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Title |
Reciprocal altruism in Papio anubis |
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Journal Article |
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Year |
1977 |
Publication |
Nature |
Abbreviated Journal |
Nature |
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265 |
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441-445 |
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10.1038/265441a0 |
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Equine Behaviour @ team @ |
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4840 |
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Author |
Adler, L.L.; Adler, H.E. |
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Title |
Ontogeny of observational learning in the dog (Canis familiaris) |
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Journal Article |
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Year |
1977 |
Publication |
Developmental Psychobiology |
Abbreviated Journal |
Dev Psychobiol |
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Volume |
10 |
Issue |
3 |
Pages |
267-271 |
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Keywords |
Animals; Dogs/*physiology; Female; Learning/*physiology; Male; Vision, Ocular/physiology |
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Abstract |
A split-litter technique was used to test observational learning in 4 litters of Miniature Dachshund puppies, 21, 28, 38, and 60 days old at the beginning of the experiment. In one side of a duplicate cage, one puppy of a litter, the demonstrator, learned to pull in a food cart on a runner by means of a ribbon, while another puppy, the observer, watched from an adjacent compartment, separated by a wire screen. Observational learning was demonstrated by the saving in time for the 1st trial when the observer was given the same problem to solve. Maturation, particularly the development of visual function and motor coordination, set a lower age limit for the emergence of observational learning. |
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0012-1630 |
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PMID:863122 |
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Equine Behaviour @ team @ |
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5186 |
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Author |
Seyfarth, R.M. |
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Title |
A model of social grooming among adult female monkeys |
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Journal Article |
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Year |
1977 |
Publication |
Journal of Theoretical Biology |
Abbreviated Journal |
J. Theor. Biol. |
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Volume |
65 |
Issue |
4 |
Pages |
671-698 |
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Keywords |
Animals; Behavior, Animal; Female; *Grooming; Haplorhini/*physiology; *Models, Biological; Reproduction; Social Dominance; Time Factors |
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Abstract |
Grooming networks among adult female monkeys exhibit two similar features across a number of different species. High-ranking animals receive more grooming than others, and the majority of grooming occurs between females of adjacent rank. A theoretical model which duplicates these features is presented, and the properties of the model are used to explain the possible causation and function of female grooming behaviour. The model illustrates how relatively simple principles governing the behaviour of individuals may be used to explain more complex aspects of the social structure of non-human primate groups. |
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0022-5193 |
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PMID:406485 |
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Equine Behaviour @ team @ |
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5259 |
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