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Author |
HUGHES RD et al, |
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Title |
Interactions between Camague horses and horseflies |
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Journal Article |
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Year |
1981 |
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Abbreviated Journal |
Bull Entomol Res 71 |
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227-242 |
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Notes |
from Professor Hans Klingels Equine Reference List |
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no |
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1210 |
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Author |
Leblanc Ma, B.M. |
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Title |
Mise au point d`une épreuve destinée de la reconnaissance du jeune par la mère chez chaval |
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Journal Article |
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Year |
1981 |
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Abbreviated Journal |
Biol Beh |
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Volume |
6 |
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283-290 |
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from Professor Hans Klingels Equine Reference List |
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no |
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1342 |
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Author |
Prescott J, |
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Title |
Suckling behavior of Llama and Chapman's Zebra in captivity |
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Journal Article |
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Year |
1981 |
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Abbreviated Journal |
Appl Anim Ethol |
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Volume |
7 |
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Pages |
293-299 |
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from Professor Hans Klingels Equine Reference List |
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no |
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1483 |
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Author |
Rau Re, |
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Title |
Zur Geschichte und Präparation der Mainzer Quaggas |
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Journal Article |
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Year |
1981 |
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Abbreviated Journal |
Mainzer Naturw Archiv |
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19 |
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221-236 |
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Notes |
from Professor Hans Klingels Equine Reference List |
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no |
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Call Number |
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Serial |
1498 |
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Author |
TURNER JR JW et al, |
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Title |
Elimination marking behavior in feral horses |
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Journal Article |
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Year |
1981 |
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Abbreviated Journal |
Can J Zool |
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Volume |
59 |
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Pages |
1561-1566 |
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Notes |
from Professor Hans Klingels Equine Reference List |
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no |
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1666 |
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Author |
Waage Jk, |
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Title |
How the zebra got its stripes – biting flies as selective agents in the evolution of zebra coloration |
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Journal Article |
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Year |
1981 |
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Abbreviated Journal |
J ent Soc S Afr |
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Volume |
44 |
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351-358 |
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Notes |
from Professor Hans Klingels Equine Reference List |
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no |
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Call Number |
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Serial |
1685 |
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Author |
Gillan DJ; Premack D; Woodruff G |
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Title |
Reasoning in the chimpanzee: I. Analogical reasoning |
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Journal Article |
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Year |
1981 |
Publication |
J. Exp. Psychol.: Anim. Behav. Process. |
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Volume |
7 |
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Pages |
1 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3063 |
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Author |
Saigo, S. |
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Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
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Journal Article |
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Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
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Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
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Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
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Abstract |
Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH. |
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English |
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ISSN |
0021-924X |
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Notes |
PMID:6270075 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. |
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Title |
Nature of the fast and slow refolding reactions of iron(III) cytochrome c |
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Journal Article |
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Year |
1981 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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Volume |
20 |
Issue |
6 |
Pages |
1622-1630 |
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Keywords |
Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis |
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Abstract |
The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding. |
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0006-2960 |
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PMID:6261802 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3809 |
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Author |
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 |
Type |
Journal Article |
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Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
113 |
Issue |
3 |
Pages |
425-433 |
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Keywords |
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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Abstract |
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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Call Number |
Equine Behaviour @ team @ |
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3810 |
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