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Author |
Saigo, S. |
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Title |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
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Journal Article |
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Year |
1981 |
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Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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669 |
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1 |
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13-20 |
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Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
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Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization. |
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0006-3002 |
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PMID:6271238 |
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refbase @ user @ |
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3871 |
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Author |
Kihara, H. |
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Title |
Comparison of the redox reactions of various types of cytochrome c with iron hexacyanides |
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Journal Article |
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Year |
1981 |
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Biochimica et Biophysica Acta (BBA) – Bioenergetics |
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634 |
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93-104 |
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Keywords |
Cytochrome c; Redox reaction; Iron hexacyanide; Temperature jump; Electron transfer |
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Abstract |
The dynamic behavior of various types of cytochromes c in the redox reaction with iron hexacyanides was studied using a temperature-jump method in order to elucidate the molecular mechanism of the redox reaction of cytochromes with their oxidoreductants. Transmittance after the temperature jump changed through a single exponential decay for all cytochromes investigated. Under a constant concentration of anion, the redox reaction of various types of cytochrome c with iron hexacyanides was analyzed according to the scheme: Ki=kt/k-i (i=1,2,3) where C(III) and C(II) are ferric and ferrous cytochromes, respectively, Fe(III) and Fe(II) are ferri- and ferrocyanides, respectively, C(III) [middle dot] Fe(II) is the ferricytochrome-ferrocyanide complex and C(II) [middle dot] Fe(III) is the ferrocytochrome-ferricyanide complex. When step B is slower than the other two steps A and C, τ-1 can be represented approximately as where the bar over the variables denotes the equilibrium value. In a large excess of ferrocyanide against cytochrome, we can estimate k2, k-2, K1 and K3 independently. In the case of horse cytochrome c at 18[degree sign]C in 0.1 M phosphate buffer at pH 7 with 0.3 M KNO3, the estimated parameters are k2 = 100 +/- 50 s-1, k-2 = (3.5 +/- 1.0) [middle dot] 103 s-1, K1 = 15 +/- 7 M-1 and K3 = (8.5 +/- 1.5) [middle dot] 10-4 M. From the same experiments for seven cytochromes (cytochrome c from horse, tuna, Candida krusei, Saccharomyces oviformis, Rhodospirillum rubrum cytochrome c2, Spirulina platensis cytochrome c-554 and Thermus thermophilus cytochrome c-552), the following results can be deduced. (1) Each parameter defined in the scheme above (k2, k-2, K1, K3) diverged beyond the error range. Above all, k2 values of cytochromes c-554 and c-552 are as large as 1 [middle dot] 104 s-1 and much larger than those for the other cytochromes (to 50 approx. 700 S-1). (2) The variance of k2K1 and k-2/K3 are relatively less than the variances of individual parameters (k2, k-2, K1 and K3), which suggests that the values of k2K1 and k-2/K3 have been conserved during the course of evolution. |
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refbase @ user @ |
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3980 |
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COUGOUILLE-GAUFFRETEAU B et al, |
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Title |
Research on the consequences of the injection of male hormones... |
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1981 |
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Comptes red Seanc Acad Sci |
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292 |
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1073-1076 |
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from Professor Hans Klingels Equine Reference List |
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993 |
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Hoyt Df, T.C. |
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Title |
Gait and the energetics of locomotion in horses |
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1981 |
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Nature |
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292 |
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239-240 |
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from Professor Hans Klingels Equine Reference List |
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no |
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1205 |
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Axelrod, R.; Hamilton, W.D. |
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Title |
The evolution of cooperation |
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Journal Article |
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Year |
1981 |
Publication |
Science |
Abbreviated Journal |
Science |
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Volume |
211 |
Issue |
4489 |
Pages |
1390-1396 |
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Cooperation in organisms, whether bacteria or primates, has been a difficulty for evolutionary theory since Darwin. On the assumption that interactions between pairs of individuals occur on a probabilistic basis, a model is developed based on the concept of an evolutionarily stable strategy in the context of the Prisoner's Dilemma game. Deductions from the model, and the results of a computer tournament show how cooperation based on reciprocity can get started in an asocial world, can thrive while interacting with a wide range of other strategies, and can resist invasion once fully established. Potential applications include specific aspects of territoriality, mating, and disease. |
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10.1126/science.7466396 |
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Equine Behaviour @ team @ |
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4933 |
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Mace, G.M.; Harvey, P.H.; Clutton-Brock, T.H. |
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Title |
Brain size and ecology in small mammals |
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Journal Article |
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Year |
1981 |
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Journal of Zoology |
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J Zool |
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193 |
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3 |
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333-354 |
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Relative brain size (measured as gross brain size after body size effects are removed) differs systematically between families of rodents, insectivores and lagomorphs. The Sciuridae have the largest relative brain size, the Soricidae and Bathyergidae the smallest. These results are discussed and compared with previous analyses of relative brain sizes among primates and bats. These differences complicate comparisons between relative brain size across phylogenetically diverse species and attempts to relate differences in relative brain size to ecological variables. To overcome these problems, best fit relationships were estimated for each family, and values for each genus were expressed as deviations from the lines of best fit. We refer to these values as Comparative Brain Size (CBS). Differences in CBS are related to differences in habitat type (forest-dwelling genera have larger CBS' than grassland forms), in diet (folivores have smaller CBS' than generalists or insectivores, frugivores and granivores), in zonation (arboreal genera have larger CBS' than terrestrial ones) and in activity timing (nocturnal genera have larger CBS' than dirurnal ones). However, these ecological categories are interrelated and, when the effects of other ecological differences are taken into account using analyses of variance, only the differences associated with diet, and possibly habitat remain. |
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Blackwell Publishing Ltd |
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1469-7998 |
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Equine Behaviour @ team @ |
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5455 |
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Author |
Hendricks, J.C.; Morrison, A.R. |
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Title |
Normal and abnormal sleep in mammals |
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Journal Article |
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1981 |
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Journal of the American Veterinary Medical Association |
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J Am Vet Med Assoc |
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178 |
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2 |
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121-126 |
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Animals; Cat Diseases/physiopathology; Cats; Cattle; Dog Diseases/physiopathology; Dogs; Dreams; Horses/physiology; Humans; Narcolepsy/physiopathology/veterinary; Sleep/*physiology; Sleep Apnea Syndromes/physiopathology/veterinary; Sleep Disorders/physiopathology/*veterinary; Sleep, REM/physiology |
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0003-1488 |
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PMID:7204232 |
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refbase @ user @ |
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101 |
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Grubb P, |
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Equus burchelli |
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1981 |
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Mammalia |
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157 |
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1-9 |
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from Professor Hans Klingels Equine Reference List |
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1138 |
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Partridge, B.L. |
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Title |
Internal dynamics and the interrelations of fish in schools |
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Year |
1981 |
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Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology |
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J Comp Physiol Sensory Neural Behav Physiol |
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144 |
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3 |
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313-325 |
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The three-dimensional structure of schools of saithe (Pollachius virens) and the interactions between individuals over time were analyzed in 12,240 frames of videotape sampled at 2.7 Hz. Time series analyses of the interactions between identified individuals allowed testing of assumptions of anonymity vs. leadership in schools and investigation of the transfer of information between individuals by which collective decisions are made. Results include the following:1.Saithe match changes in both swimming direction and speed of their neighbors but correlations are greater for swimming speed. Average speed of the school does not greatly affect correlations between neighboring fish although the reaction latencies may be somewhat increased. As shown previously (Partridge et al. 1980) nearest neighbor distance (NND) decreases with increasing school velocity.2.Saithe simultaneously match the headings and swimming speeds of at least their first two nearest neighbors within the school (NN1 and NN2). Partialling out the correlation between a fish's neighbors demonstrates that a fish's correlation to his second nearest neighbor (NN2) is not simply a transitive function of mutual correlation between the NN1 and NN2.3.Several sources of individual variation in schooling performance were examined. In all respects except one, that of preferred positions within the school, saithe showed no individual differences, i.e., some were not “better schoolers” than others. Although fish in the school differed in length by up to a factor of 2.5, no size related effects in NND or nearest neighbor positioning were found.4.Single Linkage Cluster Analysis (SLCA) of the cross-correlations of fishs' swimming speeds and directions demonstrated quantitatively the existence of subgroups within schools if they contain more than 10-11 members. Subgroups acting more-or-less independently in terms of short term variations in speed and direction nonetheless remained within the school as a whole and were not often apparent to observers since members of one group interdigitated with those of another. How individuals know to which subgroup they belong remains unanswered. |
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2063 |
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Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
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Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
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Journal Article |
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1981 |
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European Journal of Biochemistry / FEBS |
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Eur J Biochem |
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113 |
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3 |
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425-433 |
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Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism |
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Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion. |
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0014-2956 |
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PMID:7011796 |
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Equine Behaviour @ team @ |
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3810 |
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