Records |
Author |
Dyson, H.J.; Beattie, J.K. |
Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
Type |
Journal Article |
Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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ISSN |
0021-9258 |
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PMID:6277891 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Saigo, S. |
Title |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
Type |
Journal Article |
Year |
1981 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
Volume |
669 |
Issue |
1 |
Pages |
13-20 |
Keywords |
Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
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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no |
Call Number |
refbase @ user @ |
Serial |
3871 |
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Author |
Saigo, S. |
Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
Type |
Journal Article |
Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
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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Notes |
PMID:6270075 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Henning, J.M.; Zentall, T.R. |
Title |
Imitation, social facilitation, and the effects of ACTH 4-10 on rats' bar-pressing behavior |
Type |
Journal Article |
Year |
1981 |
Publication |
The American journal of psychology |
Abbreviated Journal |
Am J Psychol |
Volume |
94 |
Issue |
1 |
Pages |
125-134 |
Keywords |
Adrenocorticotropic Hormone/*pharmacology; Animals; Conditioning, Operant/*drug effects; Dose-Response Relationship, Drug; Extinction, Psychological/drug effects; Imitative Behavior/*drug effects; Male; Peptide Fragments/*pharmacology; Rats; *Social Facilitation |
Abstract |
The effects of ACTH 4-10 on rats' imitation learning was examined during the acquisition and extinction of a bar-press response for water reinforcement. Rats were exposed to either a bar-pressing conspecific (OB), an experimentally naive conspecific (ON), or an empty box (OE) during bar-press acquisition. In a factorial design, each rat was then exposed to one of the same three conditions during extinction. An 80 mcg dose of ACTH 4-10 was administered to half of the rats in each group prior to observation. Performance differences during acquisition were generally small, but significant performance differences during extinction were found. Social facilitation was indicated by the finding that rats extinguished in the presence of a conspecific exhibited significantly greater resistance to extinction than rats extinguished in the presence of an empty box. An imitation effect was also found. Rats that observed a bar-pressing conspecific during both acquisition and extinction (group OB-OB) showed significantly greater resistance top extinction than did groups OB-ON, CB-OE, or OE-OE. There were no significant effects of the hormone, however, relative to saline controls. |
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ISSN |
0002-9556 |
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Notes |
PMID:6263117 |
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no |
Call Number |
refbase @ user @ |
Serial |
267 |
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Author |
Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. |
Title |
Nature of the fast and slow refolding reactions of iron(III) cytochrome c |
Type |
Journal Article |
Year |
1981 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
Volume |
20 |
Issue |
6 |
Pages |
1622-1630 |
Keywords |
Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis |
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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Notes |
PMID:6261802 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3809 |
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Author |
Tumova, B. |
Title |
Equine influenza--a segment in influenza virus ecology |
Type |
Journal Article |
Year |
1980 |
Publication |
Comparative Immunology, Microbiology and Infectious Diseases |
Abbreviated Journal |
Comp Immunol Microbiol Infect Dis |
Volume |
3 |
Issue |
1-2 |
Pages |
45-59 |
Keywords |
Animals; Antigens, Viral; Genes, Viral; Horse Diseases/*microbiology; Horses; Influenza A virus/immunology/pathogenicity/*physiology; Orthomyxoviridae Infections/microbiology/*veterinary; Viral Proteins/analysis |
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ISSN |
0147-9571 |
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Notes |
PMID:6258849 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
2691 |
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Author |
Milouchine, V.N. |
Title |
The role of WHO in international studies on the ecology of influenza in animals |
Type |
Journal Article |
Year |
1980 |
Publication |
Comparative Immunology, Microbiology and Infectious Diseases |
Abbreviated Journal |
Comp Immunol Microbiol Infect Dis |
Volume |
3 |
Issue |
1-2 |
Pages |
25-31 |
Keywords |
Animals; Birds/microbiology; Horses/microbiology; Humans; Influenza A virus/*isolation & purification/physiology; Orthomyxoviridae Infections/microbiology/*veterinary; Swine/microbiology; World Health Organization |
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0147-9571 |
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PMID:6258848 |
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no |
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Equine Behaviour @ team @ |
Serial |
2692 |
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Author |
Tobin, T.; Combie, J.D. |
Title |
Performance testing in horses: a review of the role of simple behavioral models in the design of performance experiments |
Type |
Journal Article |
Year |
1982 |
Publication |
Journal of Veterinary Pharmacology and Therapeutics |
Abbreviated Journal |
J Vet Pharmacol Ther |
Volume |
5 |
Issue |
2 |
Pages |
105-118 |
Keywords |
Analgesics, Opioid/pharmacology; Animals; Apomorphine/pharmacology; Behavior, Animal/*drug effects; Dose-Response Relationship, Drug; Fentanyl/pharmacology; Horses/*physiology; Methylphenidate/pharmacology; *Models, Biological; Motor Activity/drug effects |
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0140-7783 |
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PMID:6125601 |
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no |
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refbase @ user @ |
Serial |
1957 |
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Author |
Alexander, F.; Horner, M.W.; Moss, M.S. |
Title |
The salivary secretion and clearance in the horse of chloral hydrate and its metabolites |
Type |
Journal Article |
Year |
1967 |
Publication |
Biochemical pharmacology |
Abbreviated Journal |
Biochem Pharmacol |
Volume |
16 |
Issue |
7 |
Pages |
1305-1311 |
Keywords |
Animals; Chloral Hydrate/blood/*metabolism/urine; Chromatography, Gas; Ethanol/blood/urine; Horses; Male; Parotid Gland/metabolism; Saliva/*analysis; Trichloroacetic Acid/blood/urine |
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0006-2952 |
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PMID:6053598 |
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no |
Call Number |
refbase @ user @ |
Serial |
118 |
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Author |
Washino, R.K.; Tempelis, C.H. |
Title |
Host-feeding patterns of Anopheles freeborni in the Sacramento Valley, California |
Type |
Journal Article |
Year |
1967 |
Publication |
Journal of Medical Entomology |
Abbreviated Journal |
J Med Entomol |
Volume |
4 |
Issue |
3 |
Pages |
311-314 |
Keywords |
Animals; Anopheles/*growth & development; California; Cats; Cattle; Dogs; Ecology; Horses; Humans; *Insect Vectors; Rabbits; Rodentia; Swine |
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0022-2585 |
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PMID:6052143 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
2745 |
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