| Records |
| Author |
Syme, G.J.; Syme, L.A. |
| Title |
The concept of spatial leadership in farm animals: An experiment with sheep |
Type |
Journal Article |
| Year |
1975 |
Publication |
Animal Behaviour. |
Abbreviated Journal |
Anim. Behav. |
| Volume |
23 |
Issue |
Part 4 |
Pages  |
921-925 |
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| Abstract |
The concept of spatial leadership as applied to farm animals is discussed with particular emphasis on methodological problems. Using three experimental procedures forced spatial leadership orders were measured in a group of Romney ewes. Comparisons between orders showed the effects of both the different experimental tasks and the social context on leadership structure. Both these variables were found to affect the orders obtained. The results are interpreted in terms of the utility of the concept of spatial leadership in domestic animals and the necessity for more systematic procedural investigations in this area. |
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2039 |
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Sivak, J.G.; Allen, D.B. |
| Title |
An evaluation of the “ramp” retina of the horse eye |
Type |
Journal Article |
| Year |
1975 |
Publication |
Vision Research |
Abbreviated Journal |
Vision Res |
| Volume |
15 |
Issue |
12 |
Pages |
1353-1356 |
| 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 |
| 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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English |
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0042-6989 |
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PMID:1210017 |
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no |
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Equine Behaviour @ team @ |
Serial |
3647 |
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| Author |
Jallon, J.M.; Risler, Y.; Iwatsubo, M. |
| Title |
Beef liver L-Glutamate dehydrogenase mechanism: presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH |
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Journal Article |
| Year |
1975 |
Publication |
Biochemical and biophysical research communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
| Volume |
67 |
Issue |
4 |
Pages |
1527-1536 |
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Animals; Cattle; Glutamate Dehydrogenase/*metabolism; Ketoglutaric Acids; Kinetics; Liver/*enzymology; Nadp; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet |
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0006-291X |
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PMID:1038 |
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Admin @ knut @ |
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21 |
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Schmoldt, A.; Benthe, H.F.; Haberland, G. |
| Title |
Digitoxin metabolism by rat liver microsomes |
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Journal Article |
| Year |
1975 |
Publication |
Biochemical pharmacology |
Abbreviated Journal |
Biochem Pharmacol |
| Volume |
24 |
Issue |
17 |
Pages |
1639-1641 |
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Animals; Chromatography, Thin Layer; Digitoxigenin/metabolism; Digitoxin/*metabolism; Hydroxylation; Male; Microsomes, Liver/*metabolism; NADP/metabolism; Rats; Time Factors |
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0006-2952 |
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PMID:10 |
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no |
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Admin @ knut @ |
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20 |
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| Author |
Dunn, M.F.; Branlant, G. |
| Title |
Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation |
Type |
Journal Article |
| Year |
1975 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
| Volume |
14 |
Issue |
14 |
Pages |
3176-3182 |
| 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 |
| 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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0006-2960 |
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PMID:238585 |
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Equine Behaviour @ team @ |
Serial |
3817 |
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