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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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0021-924X |
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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 |
Type |
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 |
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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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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 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
669 |
Issue |
1 |
Pages |
13-20 |
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Keywords |
Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
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Abstract |
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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Notes |
PMID:6271238 |
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Call Number |
refbase @ user @ |
Serial |
3871 |
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Author |
Boice, R. |
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Title |
Behavioral comparability of wild and domesticated rats |
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Journal Article |
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Year |
1981 |
Publication |
Behavior Genetics |
Abbreviated Journal |
Behav Genet |
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Volume |
11 |
Issue |
5 |
Pages |
545-553 |
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Keywords |
Animals; *Behavior, Animal; Female; Genetics, Behavioral; Intelligence; Learning; Male; Rats/*genetics |
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Abstract |
The oft-repeated concern for the lack of behavioral comparability of domestic rats with wild forms of Rattus norvegicus is unfounded. Laboratory rats appear to show the potential for all wild-type behaviors, including the most dramatic social postures. Moreover, domestics are capable of assuming a feral existence without difficulty, one where they readily behave in a fashion indistinguishable from wild rats. The one behavioral difference that is clearly established concerns performance in laboratory learning paradigms. The superiority of domestics in these laboratory tasks speaks more to quieting the concerns of degeneracy theorists than to problems of using domestic Norway rats as subjects representative of their species. |
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ISSN |
0001-8244 |
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Notes |
PMID:7325955 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4144 |
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Author |
Hoff, M.P.; Nadler, R.D.; Maple, T.L. |
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Title |
Development of infant independence in a captive group of lowland gorillas |
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Journal Article |
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Year |
1981 |
Publication |
Developmental Psychobiology |
Abbreviated Journal |
Dev Psychobiol |
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Volume |
14 |
Issue |
3 |
Pages |
251-265 |
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Keywords |
Animals; *Dependency (Psychology); Female; Gorilla gorilla/*growth & development; Male; Maternal Behavior; *Personality; Sex Factors; Social Behavior; Weaning |
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Abstract |
In March 1976, 3 lowlands gorillas (Gorilla gorilla gorilla) were born to primiparous females living with an adult male in a large compound at the field station of the Yerkes Regional Primate Research Center of Emory University. Observations of parent and infant behavior began at the birth of the infants, using several methods of data collection. This report focuses on the development of independence in these infants over the 1st 1 1/2 years of life. As expected, measures of mother-infant contact and proximity decreased with age. Several measures suggested that infant independence developed as an interactive process between mothers and infants, with primary responsibility changing over the months of study. Maternal behaviors that served to maintain mother-infant contact were found to decrease with age, with an eventual shift to infant responsibility for contact maintenance. Additionally, the adult male appeared to influence developing independence as reflected in the maternal protectiveness evoked by his behavior. |
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0012-1630 |
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Notes |
PMID:7262467 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4170 |
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Author |
Bernstein, I.S.; Dobrofsky, M. |
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Title |
Compensatory social responses of older pigtailed monkeys to maternal separation |
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Journal Article |
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Year |
1981 |
Publication |
Developmental Psychobiology |
Abbreviated Journal |
Dev Psychobiol |
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Volume |
14 |
Issue |
2 |
Pages |
163-168 |
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Keywords |
Animals; Dependency (Psychology); Female; Macaca nemestrina; Male; *Maternal Deprivation; *Social Behavior |
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Abstract |
Thirteen 3-5-year-old pigtailed monkeys were subjected to five 2-hr maternal separations while remaining in their normal social group. Significant changes in activity profiles were noted during separation and reunion phases. This suggests the continued social dependence of older offspring upon the matriarch. The shift in social activities reflected attempts by the juvenile and adolescent subjects to compensate for maternal absence by intensification of other affiliative social behavior and avoidance of potentially socially disruptive situation. The subjects oriented more towards kin in the absence of the matriarch, but actual time with kin decreased. Upon the return of the matriarch, the intensified some responses depressed during her absence and returned to preseparation social relationships. Play and aggressive responses declined whereas social approaches increased during maternal absences. Submissive responses declined upon the return of the matriarch, and play increased. The subjects also showed a marked, temporary increase of direct interaction, largely sniffing and grooming, with the matriarch upon her return. |
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0012-1630 |
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PMID:7202854 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4171 |
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