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Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K. |
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Title |
Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide |
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Journal Article |
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Year |
1977 |
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Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume  |
460 |
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3 |
Pages |
480-489 |
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Keywords |
Animals; Bacteria; *Cytochrome c Group; *Ferrocyanides; Horses; Kinetics; Mathematics; Oxidation-Reduction; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics |
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Abstract |
The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. (Formula: see text.) Thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. The results of this showed that (1) the redox potential of cytochrome c-552, + 0.19 V, is markedly less than that of horse heart cytochrome c. (2) deltaHox of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) deltaSox and deltaSred of cytochrome c-552 are more negative than those of horse heart cytochrome c. (4) kred of cytochrome c-552 is much lower than that of horse heart cytochrome c at room temperature. |
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0006-3002 |
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PMID:195599 |
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Call Number |
Equine Behaviour @ team @ |
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3815 |
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Author |
Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K.; Oshima, T. |
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Title |
Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide |
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Journal Article |
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Year |
1977 |
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Biochimica et Biophysica Acta (BBA) – Bioenergetics |
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Volume |
460 |
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3 |
Pages |
480-489 |
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Abstract |
The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. Thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. The results of this showed that (1) the redox potential of cytochrome c-552,+0.19 V, is markedly less than that of horse heart cytochrome c. (2) [up triangle, open]Hox++ of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) [up triangle, open]Hox++ and [up triangle, open]Sred++ of cytoochrome c-552 are more negative than those of horse heart cytochrome c. (4) kred of cytochrome c-552 is much lower than that of horse heart cytochrome c at room temperature. |
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refbase @ user @ |
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3986 |
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Author |
Levy, J. |
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Title |
The mammalian brain and the adaptive advantage of cerebral asymmetry |
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Journal Article |
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Year |
1977 |
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Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
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299 |
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264-272 |
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Keywords |
*Adaptation, Physiological; Adaptation, Psychological/physiology; Animals; Behavior, Animal/physiology; Brain/*physiology; Cognition/physiology; Dominance, Cerebral/*physiology; *Evolution; Humans; Intelligence; Perception/physiology |
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0077-8923 |
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PMID:280207 |
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Equine Behaviour @ team @ |
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4137 |
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Author |
Packer, C. |
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Title |
Reciprocal altruism in Papio anubis |
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Journal Article |
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1977 |
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Nature |
Abbreviated Journal |
Nature |
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265 |
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Pages |
441-445 |
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10.1038/265441a0 |
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Equine Behaviour @ team @ |
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4840 |
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Author |
Tsong, T.Y. |
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Title |
Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
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Journal Article |
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1977 |
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The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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252 |
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24 |
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8778-8780 |
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*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
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Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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PMID:200618 |
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refbase @ user @ |
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3882 |
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Author |
Alexander, R, MCN et al |
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Title |
Fast locomotion of some african ungulates |
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Journal Article |
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Year |
1977 |
Publication |
Journal of Zoology |
Abbreviated Journal |
J Zool |
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Volume |
183 |
Issue |
3 |
Pages |
291-300 |
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Abstract |
ABSTRACT
Ten species of ungulate were filmed, galloping in their natural habitat. They ranged in size from Thomson's gazelle (about 20 kg) to giraffe (about 1000 kg). They were pursued to make them run as fast as possible. The films have been analysed to determine speed, stride frequency, stride and step lengths, and duty factors. The dependence of these quantities on body size is discussed.
Summary:
Fast locomotion of zebra, giraffe, warthog and seven species of Bovidae has been studied. The animals were filmed from a pursuing vehicle while galloping in their natural habitat.
Stride frequency was more closely correlated with limb length (represented by hip height) than with body mass. Mean stride frequency was proportional to (hip height)-0·51 and maximum stride frequency to (hip height) -0·63.
Maximum speed was between 10 and 14 m s -1 for all species except buffalo (7 m s -1). It was not significantly correlated with body mass.
Since the small species ran at least as fast as the large ones they attained higher Froude numbers. Relative stride length was approximately 1·8 (Froude number)0·39 for all species, irrespective of size. Relative step length was approximately 0·65 (Froude number)0·2, both for the fore feet and for the hind ones. The vertical forces exerted by the feet are proportional to (body weight)×(Froude number)0·2 so the forces at maximum speed are larger multiples of body weight for small species than for large ones. |
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Notes |
from Prof. Hans Klingels Equine Reference List |
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refbase @ user @ |
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130 |
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Author |
Bard Jbl, |
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Title |
A unity underlying the different zebra stripping patterns |
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Journal Article |
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1977 |
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J Zool Lond |
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183 |
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527-539 |
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from Professor Hans Klingels Equine Reference List |
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923 |
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Author |
Zeeb K, |
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Title |
Comparison du comportement des chevaux et des resultats du dressage au cirque |
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Journal Article |
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1977 |
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Ann Med Vet |
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121 |
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37-38 |
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from Professor Hans Klingels Equine Reference List |
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1749 |
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Nitschelm D, H.V.D.C. |
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Title |
The influence of chlormadinone acetate treatment on the concentration of some stereoids in the blood, on the ovarian activity and on.. |
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1977 |
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Tijdschr Diergeneesk |
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102 |
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861-872 |
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from Professor Hans Klingels Equine Reference List |
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1419 |
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Author |
Nitschelm D, H.V.D.C. |
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Title |
The influence of chlormadinone acetate treatment on the concentration of some stereoids in the blood, on the ovarian activity, and on the sexual behaviour of the.. |
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1977 |
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Tijdschr Diergeneesk |
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102 |
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61-872 |
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from Professor Hans Klingels Equine Reference List |
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1420 |
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