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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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0021-924X |
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PMID:6270075 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Henning, J.M.; Zentall, T.R. |
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Title |
Imitation, social facilitation, and the effects of ACTH 4-10 on rats' bar-pressing behavior |
Type |
Journal Article |
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Year |
1981 |
Publication |
The American journal of psychology |
Abbreviated Journal |
Am J Psychol |
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Volume |
94 |
Issue |
1 |
Pages |
125-134 |
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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 |
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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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Call Number |
refbase @ user @ |
Serial |
267 |
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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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ISSN |
0006-2960 |
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Notes |
PMID:6261802 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3809 |
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Author |
Hasumi, H. |
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Title |
Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method |
Type |
Journal Article |
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Year |
1980 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
626 |
Issue |
2 |
Pages |
265-276 |
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Keywords |
Circular Dichroism; *Cytochrome c Group; Hydrogen-Ion Concentration; Isomerism; Kinetics; Spectrophotometry |
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Abstract |
The isomerization of horse-heart ferricytochrome c caused by varying pH was kinetically studied by using circular dichroism (CD) and optical absorption stopped-flow techniques. In the pH range of 7--13, the existence of the three different forms of ferricytochrome c (pH less than 10, pH 10--12, and pH greater than 12) was indicated from the statistical difference CD spectra. On the basis of analyses of the stopped-flow traces in the near-ultraviolet and Soret wavelength regions, the isomerization of ferricytochrome c from neutral form to the above three alkaline forms was interpreted as follows (1) below pH 10, the replacement of the intrinsic ligand of methionine residue by lysine residue occurs; (2) between pH 10 and 12, the uncoupling of the polypeptide chain from close proximity of the heme group occurs first, followed by the interconversion of the intrinsic ligands; and (3) above pH 12, hydroxide form of ferricytochrome c is formed, though the replacement of the intrinsic ligand by extrinsic ligands may occur via different routes from those below pH 12. The CD changes at 288 nm and in the Soret region caused by the pH-jump (down) from pH 6.0 to 1.6 were compared with the appearance of the 620-nm absorption band ascribed to the formation of the high-spin form of ferricytochrome c. Both CD and absorption changes indicated that the isomerization at pH 1.6 consisted of two processes: one proceeded within the dead-time (about 2 ms) of the stopped-flow apparatus and the other proceeded at a determinable rate with the apparatus. On the basis of these results, the isomerization of ferricytochrome c at pH 1.6 was explained as follows: (1) the transition from the low-spin form to the high-spin forms occurs within about 2 ms, the dead-time of the stopped-flow apparatus; and (2) the polypeptide chain is unfolded after the formation of the high-spin form. |
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0006-3002 |
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Notes |
PMID:6260152 |
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Call Number |
refbase @ user @ |
Serial |
3876 |
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Author |
Tumova, B. |
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Title |
Equine influenza--a segment in influenza virus ecology |
Type |
Journal Article |
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Year |
1980 |
Publication |
Comparative Immunology, Microbiology and Infectious Diseases |
Abbreviated Journal |
Comp Immunol Microbiol Infect Dis |
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Volume |
3 |
Issue |
1-2 |
Pages |
45-59 |
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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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English |
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ISSN |
0147-9571 |
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Notes |
PMID:6258849 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2691 |
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Author |
Milouchine, V.N. |
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Title |
The role of WHO in international studies on the ecology of influenza in animals |
Type |
Journal Article |
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Year |
1980 |
Publication |
Comparative Immunology, Microbiology and Infectious Diseases |
Abbreviated Journal |
Comp Immunol Microbiol Infect Dis |
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Volume |
3 |
Issue |
1-2 |
Pages |
25-31 |
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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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Call Number |
Equine Behaviour @ team @ |
Serial |
2692 |
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Author |
Dunbar, K.; MacLeod, C.M. |
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Title |
A horse race of a different color: Stroop interference patterns with transformed words |
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Journal Article |
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Year |
1984 |
Publication |
Journal of Experimental Psychology. Human Perception and Performance |
Abbreviated Journal |
J Exp Psychol Hum Percept Perform |
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Volume |
10 |
Issue |
5 |
Pages |
622-639 |
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Keywords |
*Attention; *Color Perception; Discrimination Learning; Humans; Orientation; Reaction Time; Reading; *Semantics |
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Abstract |
Four experiments investigated Stroop interference using geometrically transformed words. Over experiments, reading was made increasingly difficult by manipulating orientation uncertainty and the number of noncolor words. As a consequence, time to read color words aloud increased dramatically. Yet, even when reading a color word was considerably slower than naming the color of ink in which the word was printed, Stroop interference persisted virtually unaltered. This result is incompatible with the simple horse race model widely used to explain color-word interference. When reading became extremely slow, a reversed Stroop effect--interference in reading the word due to an incongruent ink color--appeared for one transformation together with the standard Stroop interference. Whether or not the concept of automaticity is invoked, relative speed of processing the word versus the color does not provide an adequate overall explanation of the Stroop phenomenon. |
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0096-1523 |
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PMID:6238123 |
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Equine Behaviour @ team @ |
Serial |
4065 |
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Author |
Tobin, T.; Combie, J.D. |
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Title |
Performance testing in horses: a review of the role of simple behavioral models in the design of performance experiments |
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Journal Article |
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Year |
1982 |
Publication |
Journal of Veterinary Pharmacology and Therapeutics |
Abbreviated Journal |
J Vet Pharmacol Ther |
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Volume |
5 |
Issue |
2 |
Pages |
105-118 |
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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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refbase @ user @ |
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1957 |
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Author |
Alexander, F.; Horner, M.W.; Moss, M.S. |
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Title |
The salivary secretion and clearance in the horse of chloral hydrate and its metabolites |
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Journal Article |
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Year |
1967 |
Publication |
Biochemical pharmacology |
Abbreviated Journal |
Biochem Pharmacol |
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Volume |
16 |
Issue |
7 |
Pages |
1305-1311 |
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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 |
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Call Number |
refbase @ user @ |
Serial |
118 |
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Author |
Washino, R.K.; Tempelis, C.H. |
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Title |
Host-feeding patterns of Anopheles freeborni in the Sacramento Valley, California |
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Journal Article |
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Year |
1967 |
Publication |
Journal of Medical Entomology |
Abbreviated Journal |
J Med Entomol |
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Volume |
4 |
Issue |
3 |
Pages |
311-314 |
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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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Call Number |
Equine Behaviour @ team @ |
Serial |
2745 |
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