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Duncan, P.; Vigne, N. |
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Title |
The effect of group size in horses on the rate of attacks by blood-sucking flies |
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Journal Article |
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Year |
1979 |
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Animal Behaviour. |
Abbreviated Journal |
Anim. Behav. |
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27 |
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Part 2 |
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623-625 |
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763 |
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Gates, S. |
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A Study of home ranges of free ranging Exmoore ponies |
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Journal Article |
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1979 |
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Mammal Revision |
Abbreviated Journal |
Mamm. Rev. |
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9 |
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:3-18 |
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765 |
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Clutton-Brock, T.H.; Albon, S.D.; Gibson, R.M.; Guinness, F.E. |
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Title |
The logical stag: Adaptive aspects of fighting in red deer (Cervus elaphus L.) |
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Journal Article |
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Year |
1979 |
Publication |
Animal Behaviour. |
Abbreviated Journal |
Anim. Behav. |
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27 |
Issue |
Part 1 |
Pages |
211-225 |
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For red deer stags, fighting both has appreciable costs and yields considerable benefits. Up to 6% of rutting stags are permanently injured each year, while fighting success and reproductive success are closely related, within age groups as well as across them. Fighting behaviour is sensitive to changes in the potential benefits of fighting: stags fight most frequently and most intensely where potential benefits are high and tend to avoid fighting with individuals they are unlikely to beat. The relevance of these findings to theoretical models of fighting behaviour is discussed. |
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860 |
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Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M. |
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Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) |
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1979 |
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Journal of Inorganic Biochemistry |
Abbreviated Journal |
J Inorg Biochem |
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11 |
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2 |
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95-100 |
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Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism |
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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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English |
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0162-0134 |
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PMID:228006 |
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3879 |
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Kordal, R.J.; Parsons, S.M. |
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Liver alcohol dehydrogenase subunit equivalence studied by rapid sampling of alcohol product formed from sequentially bound [4α-3H]NADH |
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1979 |
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Archives of Biochemistry and Biophysics |
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194 |
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2 |
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439-448 |
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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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refbase @ user @ |
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3983 |
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