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Author |
Ayeni, J.S.O. |
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Title |
Utilization of waterholes in Tsavo National Park (East) |
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Journal Article |
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Year |
1975 |
Publication |
African Journal of Ecology |
Abbreviated Journal |
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Volume |
13 |
Issue |
3-4 |
Pages |
305-323 |
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Abstract |
Summary Utilization of waterholes by wildlife was studied between April, 1973 and July, 1974 in Tsavo National Park (East), south of the Voi river. Seasonality was an important factor which influenced the various aspects of waterhole utilization. The numbers of the herbivores utilizing the waterholes increased during the dry season but fell during the rains. Some ungulates also moved near to the artificial waterholes in the dry season but moved away from them during the rains when they drank from natural water-holes formed in clay pans filled with rain water. A basic pattern of waterhole utilization dominated by small (adult-size) species during day-time 06.00–18.00 hours and larger species at night 18.00–06.00 hours is described. The separation in times of arrival and deparature peaks of waterhole utilization, and average coincidence of percentages of paired species populations are used to show that big-game attained a measure of time-spaced ecological separation at the waterholes. The water relations of some day-time and night-time drinkers are discussed. From the baseline study the management implications of the development of additional waterholes in the park are discussed. |
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Blackwell Publishing Ltd |
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ISSN |
1365-2028 |
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Call Number |
Equine Behaviour @ team @ |
Serial  |
5364 |
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Author |
Zimen, E. |
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Title |
Social dynamics of the wolf pack |
Type |
Book Chapter |
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Year |
1975 |
Publication |
The wild canids |
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Volume |
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Pages |
336-362 |
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Publisher |
Van Nostrand Reinhold |
Place of Publication |
New York |
Editor |
Fox, M.W. |
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Call Number |
Equine Behaviour @ team @ |
Serial |
5231 |
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Author |
Stober, M.; Geiger, J.F. |
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Title |
[Lamenting “moaning” in domestic cattle] |
Type |
Journal Article |
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Year |
1975 |
Publication |
DTW. Deutsche Tierarztliche Wochenschrift |
Abbreviated Journal |
Dtsch Tierarztl Wochenschr |
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Volume |
82 |
Issue |
1 |
Pages |
10-13 |
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Keywords |
Animals; Behavior, Animal; *Cattle; Female; Personality; *Vocalization, Animal |
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German |
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Original Title |
Untersuchungen uber das klagende “Anken” beim Hausrind |
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ISSN |
0341-6593 |
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Notes |
PMID:1089525 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4173 |
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Author |
Jensen, G.D.; Gordon, B.N.; Wolfheim, J. |
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Title |
Nursing behavior in infant monkeys: a sequence analysis |
Type |
Journal Article |
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Year |
1975 |
Publication |
Behaviour |
Abbreviated Journal |
Behaviour |
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Volume |
55 |
Issue |
1-2 |
Pages |
115-127 |
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Keywords |
Animals; Dependency (Psychology); *Feeding Behavior; Female; *Macaca; Male; Sensory Deprivation; Social Behavior; Spatial Behavior |
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English |
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ISSN |
0005-7959 |
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Notes |
PMID:1191212 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4153 |
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Author |
Bergmann, H.H.; Klaus, S.; Muller, F.; Wiesner, J. |
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Title |
[Individuality and type specificity in the songs of a population of hazel grouse (Bonasa bonasia bonasia L., Tetraoninae, Phasianidae)] |
Type |
Journal Article |
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Year |
1975 |
Publication |
Behaviour |
Abbreviated Journal |
Behaviour |
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Volume |
55 |
Issue |
1-2 |
Pages |
94-114 |
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Keywords |
Animals; *Birds; Female; *Individuality; Male; Time Factors; *Vocalization, Animal |
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German |
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Original Title |
Individualitat und Artspezifitat in den Gesangsstrophen einer Population des Haselhuhns (Bonasa bonasia bonasia L., Tetraoninae, Phasianidae) |
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ISSN |
0005-7959 |
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Notes |
PMID:1191217 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4152 |
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Author |
Wood, F.E.; Cusanovich, M.A. |
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Title |
The reaction of Euglena gracilis cytochrome c-552 with nonphysiological oxidants and reductants |
Type |
Journal Article |
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Year |
1975 |
Publication |
Archives of Biochemistry and Biophysics |
Abbreviated Journal |
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Volume |
168 |
Issue |
2 |
Pages |
333-342 |
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Abstract |
The reaction of Euglena gracilis cytochrome c-552 (cytochrome f) with the nonphysiological reactants potassium ferrocyanide, potassium ferricyanide, sodium ascorbate, sodium dithionite, and Chromatium vinosum high potential nonheme iron protein was studied by stopped-flow and temperature-jump kinetic methods. The reaction of the purified, water-soluble protein with the reactants was investigated as a function of ionic strength, pH, and temperature. The results demonstrated that reduction and oxidation takes place at a negatively charged site on the cytochrome c-552 surface. Participation of specific amino acid residues in electron transfer is implicated from the pH results. The results obtained for the nonphysiological reactions of cytochrome c-552 are compared with available data for horse heart cytochrome c and Rhodospirillum rubrum cytochrome c2. The results strongly suggest that Euglena gracilis cytochrome c-552 undergoes nonphysiological oxidation and reduction by a mechanism different from that found for cytochrome c or cytochrome c2. |
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Call Number |
refbase @ user @ |
Serial |
3987 |
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Author |
Czerlinski, G.H.; Wagner, M.; Erickson, J.O.; Theorell, H. |
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Title |
Chemical relaxation studies on the system liver alcohol dehydrogenase, NADH and imidazole |
Type |
Journal Article |
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Year |
1975 |
Publication |
Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry |
Abbreviated Journal |
Acta Chem Scand B |
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Volume |
29 |
Issue |
8 |
Pages |
797-810 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Computers; Hydrogen-Ion Concentration; Imidazoles/*metabolism; Kinetics; Liver/enzymology/*metabolism; Mathematics; Models, Chemical; NAD/*metabolism; Time Factors |
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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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ISSN |
0302-4369 |
ISBN |
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Notes |
PMID:882 |
Approved |
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Call Number |
refbase @ user @ |
Serial |
3887 |
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Author |
Dunn, M.F.; Branlant, G. |
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Title |
Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation |
Type |
Journal Article |
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Year |
1975 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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Volume |
14 |
Issue |
14 |
Pages |
3176-3182 |
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Keywords |
*Alcohol Oxidoreductases/metabolism; Aldehydes/*pharmacology; Animals; Binding Sites; Enzyme Activation/drug effects; Horses; Hydrogen-Ion Concentration; Kinetics; Liver/enzymology; *NAD/analogs & derivatives/pharmacology; Oxidation-Reduction; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; *Zinc/pharmacology |
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Abstract |
1,4,5,6-Tetrahydronicotinamide adenine dinucleotide (H2NADH) has been investigated as a reduced coenzyme analog in the reaction between trans-4-N,N-dimethylaminocinnamaldehyde (I) (lambdamax 398 nm, epsilonmax 3.15 X 10-4 M-minus 1 cm-minus 1) and the horse liver alcohol dehydrogenase-NADH complex. These equilibrium binding and temperature-jump kinetic studies establish the following. (i) Substitution of H2NADH for NADH limits reaction to the reversible formation of a new chromophoric species, lambdamax 468 nm, epsilonmax 5.8 x 10-4 M-minus 1 cm-minus 1. This chromophore is demonstrated to be structurally analogous to the transient intermediate formed during the reaction of I with the enzyme-NADH complex [Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882]. (ii) The process of intermediate formation with the enzyme-NADH complex is independent of pH over the range 6.13-10.54. Although studies were limited to the pH range 5.98-8.72, a similar pH independence appears to hold for the H2NADH system. (iii) Within the ternary complex, I is bound within van der Waal's contact distance of the coenzyme nicotinamide ring. (iv) Formation of the transient intermediate does not involve covalent modification of coenzyme. Based on these findings, we conclude that zinc ion has a Lewis acid function in facilitating the chemical activation of the aldehyde carbonyl for reduction, and that reduced coenzyme plays a noncovalent effector role in this substrate activating step. |
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English |
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ISSN |
0006-2960 |
ISBN |
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Notes |
PMID:238585 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3817 |
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Author |
Bayley, P.; Martin, S.; Anson, M. |
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Title |
Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution |
Type |
Journal Article |
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Year |
1975 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
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Volume |
66 |
Issue |
1 |
Pages |
303-308 |
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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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ISSN |
0006-291X |
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Notes |
PMID:1172440 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3816 |
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Author |
Sivak, J.G.; Allen, D.B. |
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Title |
An evaluation of the “ramp” retina of the horse eye |
Type |
Journal Article |
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Year |
1975 |
Publication |
Vision Research |
Abbreviated Journal |
Vision Res |
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Volume |
15 |
Issue |
12 |
Pages |
1353-1356 |
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Keywords |
Accommodation, Ocular; Animals; Aqueous Humor/physiology; Cornea/physiology; Freezing; Horses/*anatomy & histology; Lens, Crystalline/anatomy & histology/physiology; Refraction, Ocular; Retina/*anatomy & histology; Vitreous Body/physiology |
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Abstract |
Using a rapid freezing and sectioning technique, the distance between the lens and retina of the horse eye was measured. There is no indication of a ramp retina that could serve accommodation. The pupil axis of the eye coincides with the maximum lens to retina distance. The changes in the lens-retina distance are greater below the axis than above it. Calculations were made of refractive power of the horse eye from measurements of curvature and refractive indices of the ocular tissues. These calculations agree both qualitatively and quantitatively with retinoscopic measurements on live horses. Both show that the refractive state shifts in the direction of hyperopia above and below the axis and that this shift is greater below the axis than above it. Some dynamic accommodative ability in the living eye was observed. |
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ISSN |
0042-6989 |
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Notes |
PMID:1210017 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3647 |
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