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Author |
Thor, D.H.; Holloway, W.R. |
Title |
Social memory of the male laboratory rat |
Type |
Journal Article |
Year |
1982 |
Publication |
Journal of Comparative and Physiological Psychology |
Abbreviated Journal |
J. Comp. Physiol. Psychol. |
Volume |
96 |
Issue |
6 |
Pages |
1000-1006 |
Keywords |
duration of social-investigatory behavior, measure of conspecific recognition &; social memory, male rats |
Abstract |
Used duration of social-investigatory behavior by 36 mature male Long-Evans rats as a measure of individual recognition in 5 experiments to assess social memory. In Exp I, the duration of social investigation during a 2nd exposure to the same juvenile (n[en space]=[en space]12) was directly related to the length of the interexposure interval. In Exp II, Ss were exposed to the same or different juvenile 10 min after an initial 5-min exposure to a novel juvenile; reexposure to the same juvenile elicited significantly less social investigation than an exposure to a different juvenile. Exps III and IV demonstrated that following a 5-min introductory exposure, social memory of the juvenile was relatively brief in comparison with that of mature Ss. Exp V revealed a retroactive interference effect on recently acquired memory for an individual: 12 mature Ss exposed to interpolated social experience engaged in significantly longer investigation of a juvenile than those with no interpolated social experience. The combined results suggest that (1) the rat normally engages in spontaneous learning of individual identity and (2) social memory may be a significant aspect of complex social interactions. (16 ref) (PsycINFO Database Record (c) 2006 APA, all rights reserved) |
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0021-9940 |
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Equine Behaviour @ team @ |
Serial |
5133 |
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Author |
Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
Title |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
Type |
Journal Article |
Year |
2001 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
Volume |
123 |
Issue |
27 |
Pages |
6649-6653 |
Keywords |
Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
Abstract |
We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding. |
Address |
Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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0002-7863 |
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PMID:11439052 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3788 |
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Author |
Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. |
Title |
Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c |
Type |
Journal Article |
Year |
2004 |
Publication |
The Protein Journal |
Abbreviated Journal |
Protein J |
Volume |
23 |
Issue |
8 |
Pages |
519-527 |
Keywords |
Animals; Cytochromes c/*chemistry; Enzyme Activation; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry |
Abstract |
We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal. |
Address |
Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 7/A 43100 Parma, Italy |
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ISSN |
1572-3887 |
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Notes |
PMID:15648974 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3770 |
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