Kordal, R. J., & Parsons, S. M. (1979). Liver alcohol dehydrogenase subunit equivalence studied by rapid sampling of alcohol product formed from sequentially bound [4α-3H]NADH. Archives of Biochemistry and Biophysics, 194(2), 439–448.
Abstract: Horse liver alcohol dehydrogenase has been claimed to exhibit presteady-state “half-of-the-sites” reactivity with aromatic substrates under some circumstances. To clarify the role of half-of-the-sites reactivity in liver alcohol dehydrogenase the direct sampling of the alcohol product formed immediately after initiation of the reaction was studied using a rapid sampling device and [4α-3H]NADH. Liver alcohol dehydrogenase which contained a very low mole-ratio of [4α-3H]NADH bound to one subunit of the dimer was rapidly mixed with excess 4-(2'-imidazolylazo)benzaldehyde substrate and nonradioactive NADH to initiate the reaction, which was allowed to proceed for a short time before it was quenched. If strong HClO4 quench was used isolation of total free and bound azoalcohol product was possible. If NaOH quench was used isolation only of the azoalcohol product released by the enzyme was possible since most enzyme-bound azoalcohol was reversed back to azoaldehyde by the base. The pH-jump reversal reaction also was characterized spectroscopically by stopped flow technique. Nearly fullsites reactivity was observed for reaction in either direction. Furthermore (4α-3H]NADH bound firstly to one subunit in the dimer reacted essentially identically to NADH bound secondly to the other subunit. Thus, half-of-the-sites reactivity was not observed in these experiments nor did they give any indication of liver alcohol dehydrogenase active site nonequivalence induced by coenzyme binding or reaction.
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Wilson, M. T., Silvestrini, M. C., Morpurgo, L., & Brunori, M. (1979). Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551). J Inorg Biochem, 11(2), 95–100.
Abstract: The electron transfer reactions between Rhus vernicifera stellacyanin and either horse heart cytochrome c or Pseudomonas aeruginosa cytochrome c551 were investigated by rapid reaction techniques. The time course of electron transfer is monophasic under all conditions, and thus consistent with a simple formulation of the reaction. Both stopped-flow and temperature-jump experiments yield equilibrium constants in reasonable agreement with values calculated from the redox potentials. The differences in reaction rate between the two cytochromes and stellacyanin are discussed in terms of the Marcus theory.
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Czerlinski, G. H., Erickson, J. O., & Theorell, H. (1979). Chemical relaxation studies on the horse liver alcohol dehydrogenase system. Physiol Chem Phys, 11(6), 537–569.
Abstract: Chemical relaxation studies on the system horse liver alcohol dehydrogenase, nicotinamide adenine dinucleotide, and ethanol were conducted observing fluorescence changes between 400 and 500 nm. Temperature-jump experiments were performed at pH 6.5, 7.0, 8.0, and 9.0; concentration-jump experiments at pH 9.0. The reciprocal of the slowest relaxation time was found to be linearly dependent upon the enzyme concentration for relatively low enzyme concentrations, as predicted earlier. Use of the wide pH-range necessitated expression of the four apparent dissociation constants of the catalytic reaction cycle in terms of pH-independent constants. The system was described in terms of only one (or two) catalysis-linked protons not associated with the electron transfer. Protonic steps in a buffered system are in rapid equilibrium, too fast to be measured with the equipment available. Assuming only two of the four bimolecular reaction steps in the four-step cycle are fast compared to the remaining two, six cases may be considered with six expressions for the reciprocal of the slowest relaxation time. Comparison with the experimental data revealed that the bimolecular reaction steps governing the slowest relaxation time change with pH. Above the effective time resolution of the temperature-lump instrument with fluorescence detection (0.1 msec) only one other relaxation time was detectable and only at pH 9. This relaxation time, found to be independent of the concentration of all reactants within experimental error (r = 10 +/- 5 msec), is most likely due to an interconversion among ternary complexes.
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Fiske, J. C. (1979). Behavior and learning in horses Applications in management and training. Southwestern Veterinarian, 32, 37–44.
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[No authors listed]. (1979). International Conference on Environmental Cadmium: an overview. In Environmental Health Perspectives (Vol. 28, pp. 297–30).
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Ribeiro, H. S., Larangeira, N. L., & Paiva, F. (1979). [Prevalence of Dictyocaulus arnfieldi (Cobbald, 1884) Railiet & Henry 1907, in Pantaneira breed horses of the region of Pocone, MT]. Arq Inst Biol (Sao Paulo), 46(3-4), 107–110.
Abstract: The authors sacrificed fifty-five horses originated from the “Pantanal”, lowlands in the State of Mato Grosso in two different periods, droughty period and flooded and they described for the first time the Dictyocaulus arnfieldi in Mato Grosso. Relationship between droughty and flooded periods proved not to occur.
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Miller, R. (1979). Band organisation and stability in Red Desert feral horses. In R.H. Denniston (Ed.), Proceedings of a Conference on the Ecology and Behavior of Feral Equids (pp. 113–123). Laramie: University of Wyoming.
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Sinclair, A. R. E. (1979). Serengeti: Dynamics of an Ecosystem.
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Keiper, R. R. (1979). The behaviour, ecology and social organization of the feral ponies of Assateague Island. Proc. I. Conf. Sci. Res. Nat. Parks,, .
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Powell, R. A. (1979). The dog: Its domestication and behavior : By . New York: Garland STPM Press (1978). 296 pp. $24.50. Anim. Behav., 27(Part 1), 318–1211.
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