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Mungall Ec,. (1979). Habitat preferences of Africa's recent equidae, with special reference to the extinct quagga. Symposium on the Ecology and Behavior of wild and feral Equids, Laramie, , 159–172.
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Mori, U. (1979). Ecological and sociological studies of gelada baboons. Individual relationships within a unit. Contrib Primatol, 16, 93–124.
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Mori, U. (1979). Ecological and sociological studies of gelada baboons. Inter-unit relationships. Contrib Primatol, 16, 83–92.
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Mori, U. (1979). Ecological and sociological studies of gelada baboons. Unit formation and the emergence of a new leader. Contrib Primatol, 16, 155–181.
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Moehlman Pdr,. (1979). Behavior and ecology of feral asses (Equus asinus) Diss Univ of Wisconsin. Nat. Geo. Soc. Res. Rep.,, , 405–411.
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Miller, R., & Denniston, R. H. (1979). Interband dominance in feral horses. Z. Tierpsychol., 51, 41–47.
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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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Mccort Wd,. (1979). The feral asses (Equus asinus) of Ossabaw Island, Georgia: Mating system and the effects of Vasectomies as a population. Control Procedure. Symposium on the Ecology and Behavior of wild and feral Equids, Laramie, , 71–83.
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Krzeminska, W. (1979). [The child learns about the world]. Pieleg Polozna, (7), 24–25.
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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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