| Records |
| Author |
Hendricks, J.C.; Morrison, A.R. |
| Title |
Normal and abnormal sleep in mammals |
Type |
Journal Article |
| Year |
1981 |
Publication |
Journal of the American Veterinary Medical Association |
Abbreviated Journal |
J Am Vet Med Assoc |
Volume  |
178 |
Issue |
2 |
Pages |
121-126 |
| Keywords |
Animals; Cat Diseases/physiopathology; Cats; Cattle; Dog Diseases/physiopathology; Dogs; Dreams; Horses/physiology; Humans; Narcolepsy/physiopathology/veterinary; Sleep/*physiology; Sleep Apnea Syndromes/physiopathology/veterinary; Sleep Disorders/physiopathology/*veterinary; Sleep, REM/physiology |
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English |
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| ISSN |
0003-1488 |
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| Notes |
PMID:7204232 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
101 |
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| Author |
Mace, G.M.; Harvey, P.H.; Clutton-Brock, T.H. |
| Title |
Brain size and ecology in small mammals |
Type |
Journal Article |
| Year |
1981 |
Publication |
Journal of Zoology |
Abbreviated Journal |
J Zool |
| Volume |
193 |
Issue |
3 |
Pages |
333-354 |
| Keywords |
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| Abstract |
Relative brain size (measured as gross brain size after body size effects are removed) differs systematically between families of rodents, insectivores and lagomorphs. The Sciuridae have the largest relative brain size, the Soricidae and Bathyergidae the smallest. These results are discussed and compared with previous analyses of relative brain sizes among primates and bats. These differences complicate comparisons between relative brain size across phylogenetically diverse species and attempts to relate differences in relative brain size to ecological variables. To overcome these problems, best fit relationships were estimated for each family, and values for each genus were expressed as deviations from the lines of best fit. We refer to these values as Comparative Brain Size (CBS). Differences in CBS are related to differences in habitat type (forest-dwelling genera have larger CBS' than grassland forms), in diet (folivores have smaller CBS' than generalists or insectivores, frugivores and granivores), in zonation (arboreal genera have larger CBS' than terrestrial ones) and in activity timing (nocturnal genera have larger CBS' than dirurnal ones). However, these ecological categories are interrelated and, when the effects of other ecological differences are taken into account using analyses of variance, only the differences associated with diet, and possibly habitat remain. |
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Blackwell Publishing Ltd |
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| ISSN |
1469-7998 |
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no |
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Equine Behaviour @ team @ |
Serial |
5455 |
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| Author |
Axelrod, R.; Hamilton, W.D. |
| Title |
The evolution of cooperation |
Type |
Journal Article |
| Year |
1981 |
Publication |
Science |
Abbreviated Journal |
Science |
| Volume |
211 |
Issue |
4489 |
Pages |
1390-1396 |
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| Abstract |
Cooperation in organisms, whether bacteria or primates, has been a difficulty for evolutionary theory since Darwin. On the assumption that interactions between pairs of individuals occur on a probabilistic basis, a model is developed based on the concept of an evolutionarily stable strategy in the context of the Prisoner's Dilemma game. Deductions from the model, and the results of a computer tournament show how cooperation based on reciprocity can get started in an asocial world, can thrive while interacting with a wide range of other strategies, and can resist invasion once fully established. Potential applications include specific aspects of territoriality, mating, and disease. |
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10.1126/science.7466396 |
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no |
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Equine Behaviour @ team @ |
Serial |
4933 |
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COUGOUILLE-GAUFFRETEAU B et al, |
| Title |
Research on the consequences of the injection of male hormones... |
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Journal Article |
| Year |
1981 |
Publication |
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Abbreviated Journal |
Comptes red Seanc Acad Sci |
| Volume |
292 |
Issue |
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Pages |
1073-1076 |
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| Notes |
from Professor Hans Klingels Equine Reference List |
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no |
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Serial |
993 |
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| Author |
Hoyt Df, T.C. |
| Title |
Gait and the energetics of locomotion in horses |
Type |
Journal Article |
| Year |
1981 |
Publication |
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Abbreviated Journal |
Nature |
| Volume |
292 |
Issue |
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Pages |
239-240 |
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from Professor Hans Klingels Equine Reference List |
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no |
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Serial |
1205 |
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| Author |
Kihara, H. |
| Title |
Comparison of the redox reactions of various types of cytochrome c with iron hexacyanides |
Type |
Journal Article |
| Year |
1981 |
Publication |
Biochimica et Biophysica Acta (BBA) – Bioenergetics |
Abbreviated Journal |
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| Volume |
634 |
Issue |
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Pages |
93-104 |
| Keywords |
Cytochrome c; Redox reaction; Iron hexacyanide; Temperature jump; Electron transfer |
| Abstract |
The dynamic behavior of various types of cytochromes c in the redox reaction with iron hexacyanides was studied using a temperature-jump method in order to elucidate the molecular mechanism of the redox reaction of cytochromes with their oxidoreductants. Transmittance after the temperature jump changed through a single exponential decay for all cytochromes investigated. Under a constant concentration of anion, the redox reaction of various types of cytochrome c with iron hexacyanides was analyzed according to the scheme: Ki=kt/k-i (i=1,2,3) where C(III) and C(II) are ferric and ferrous cytochromes, respectively, Fe(III) and Fe(II) are ferri- and ferrocyanides, respectively, C(III) [middle dot] Fe(II) is the ferricytochrome-ferrocyanide complex and C(II) [middle dot] Fe(III) is the ferrocytochrome-ferricyanide complex. When step B is slower than the other two steps A and C, τ-1 can be represented approximately as where the bar over the variables denotes the equilibrium value. In a large excess of ferrocyanide against cytochrome, we can estimate k2, k-2, K1 and K3 independently. In the case of horse cytochrome c at 18[degree sign]C in 0.1 M phosphate buffer at pH 7 with 0.3 M KNO3, the estimated parameters are k2 = 100 +/- 50 s-1, k-2 = (3.5 +/- 1.0) [middle dot] 103 s-1, K1 = 15 +/- 7 M-1 and K3 = (8.5 +/- 1.5) [middle dot] 10-4 M. From the same experiments for seven cytochromes (cytochrome c from horse, tuna, Candida krusei, Saccharomyces oviformis, Rhodospirillum rubrum cytochrome c2, Spirulina platensis cytochrome c-554 and Thermus thermophilus cytochrome c-552), the following results can be deduced. (1) Each parameter defined in the scheme above (k2, k-2, K1, K3) diverged beyond the error range. Above all, k2 values of cytochromes c-554 and c-552 are as large as 1 [middle dot] 104 s-1 and much larger than those for the other cytochromes (to 50 approx. 700 S-1). (2) The variance of k2K1 and k-2/K3 are relatively less than the variances of individual parameters (k2, k-2, K1 and K3), which suggests that the values of k2K1 and k-2/K3 have been conserved during the course of evolution. |
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no |
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refbase @ user @ |
Serial |
3980 |
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| Author |
Saigo, S. |
| Title |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
Type |
Journal Article |
| Year |
1981 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
| Volume |
669 |
Issue |
1 |
Pages |
13-20 |
| Keywords |
Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
| Abstract |
Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization. |
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English |
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0006-3002 |
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| Notes |
PMID:6271238 |
Approved |
no |
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refbase @ user @ |
Serial |
3871 |
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