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Author |
Czerlinski, G.H.; Erickson, J.O.; Theorell, H. |
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Title |
Chemical relaxation studies on the horse liver alcohol dehydrogenase system |
Type |
Journal Article |
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Year |
1979 |
Publication |
Physiological Chemistry and Physics |
Abbreviated Journal |
Physiol Chem Phys |
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Volume |
11 |
Issue |
6 |
Pages |
537-569 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Buffers; Electron Transport; Ethanol/metabolism; Horses; Hydrogen-Ion Concentration; Liver/*enzymology; Mathematics; NAD/metabolism; Oscillometry; Osmolar Concentration; Temperature; Time Factors |
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Abstract |
Chemical relaxation studies on the system horse liver alcohol dehydrogenase, nicotinamide adenine dinucleotide, and ethanol were conducted observing fluorescence changes between 400 and 500 nm. Temperature-jump experiments were performed at pH 6.5, 7.0, 8.0, and 9.0; concentration-jump experiments at pH 9.0. The reciprocal of the slowest relaxation time was found to be linearly dependent upon the enzyme concentration for relatively low enzyme concentrations, as predicted earlier. Use of the wide pH-range necessitated expression of the four apparent dissociation constants of the catalytic reaction cycle in terms of pH-independent constants. The system was described in terms of only one (or two) catalysis-linked protons not associated with the electron transfer. Protonic steps in a buffered system are in rapid equilibrium, too fast to be measured with the equipment available. Assuming only two of the four bimolecular reaction steps in the four-step cycle are fast compared to the remaining two, six cases may be considered with six expressions for the reciprocal of the slowest relaxation time. Comparison with the experimental data revealed that the bimolecular reaction steps governing the slowest relaxation time change with pH. Above the effective time resolution of the temperature-lump instrument with fluorescence detection (0.1 msec) only one other relaxation time was detectable and only at pH 9. This relaxation time, found to be independent of the concentration of all reactants within experimental error (r = 10 +/- 5 msec), is most likely due to an interconversion among ternary complexes. |
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0031-9325 |
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PMID:44918 |
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Call Number |
Equine Behaviour @ team @ |
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3813 |
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Author |
Chmel, L.; Hasilikova, A.; Hrasko, J.; Vlacilikova, A. |
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Title |
The influence of some ecological factors on keratinophilic fungi in the soil |
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Journal Article |
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Year |
1972 |
Publication |
Sabouraudia |
Abbreviated Journal |
Sabouraudia |
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Volume |
10 |
Issue |
1 |
Pages |
26-34 |
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Keywords |
Animals; Arthrodermataceae/growth & development/isolation & purification/metabolism; Carbohydrates; Czechoslovakia; Ecology; Fungi/growth & development/*isolation & purification/metabolism; Hair; Horses; Humic Substances; Humidity; Keratins/metabolism; Microsporum/isolation & purification; Mitosporic Fungi/isolation & purification; Phosphates; Seasons; Soil; *Soil Microbiology; Species Specificity; Temperature; Trichophyton/isolation & purification |
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0036-2174 |
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PMID:5063162 |
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Call Number |
Equine Behaviour @ team @ |
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2719 |
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Author |
Dyson, H.J.; Beattie, J.K. |
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Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
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Journal Article |
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Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
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Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
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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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0021-9258 |
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Notes |
PMID:6277891 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
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Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
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Journal Article |
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Year |
1996 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
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Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
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Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
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The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse. |
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School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, USA |
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0027-8424 |
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Notes |
PMID:8650166 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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Author |
Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
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Title |
The core of apomyoglobin E-form folds at the diffusion limit |
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Journal Article |
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Year |
1998 |
Publication |
Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
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Volume |
5 |
Issue |
5 |
Pages |
363-365 |
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Keywords |
Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
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Abstract |
The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation. |
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1072-8368 |
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Notes |
PMID:9586997 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3795 |
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Author |
Fazio, E.; Medica, P.; Cravana, C.; Giacoppo, E.; Ferlazzo, A. |
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Title |
Effect of Short-Distance Road Transport on Thyroid Function, Rectal Temperature, Body Weight and Heart Rate of Stallions |
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Conference Article |
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Year |
2008 |
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IESM 2008 |
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horses, iodothyronines, rectal temperature, body weight, heart rate, transport |
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Abstract |
Aim of study was to investigate the effects of transport stress on thyroid response, body weight, rectal temperature and heart rate changes in one hundred twenty-six healthy stallions in basal conditions, before and after short road transport. One hundred twenty-six Thoroughbreds and crossbreds stallions with previous travelling experience, aged 4 to 15 yr, were transported by road in a commercial trailer for a period of 3 h (distance <300 km). Blood samples and physiological parameters were collected at 0800 (basal I) and at 1100 (basal II), in each horse“s box, one week before the loading and transport in basal conditions, and one week later, at 0800 immediately before loading (pre-transport), and after 3 h period of transport and unloading, on their arrival at the breeding stations (post-transport), in each new horse”s box, within 30 min. Increases in circulating T3, T4 and fT4 levels (P < 0.01), but not for fT3 levels, were observed after transport, as compared to before loading values, irrespective of different breed. Lower T4 and fT4 levels were observed in basal II (P < 0.01) than basal I and before loading values (pre-transport). After transport Thoroughbreds showed higher fT3 (P < 0.05) and fT4 (P < 0.01) levels than crossbred stallions. No significant differences for T3 and T4 changes were observed. A significant increase in rectal temperature (P < 0.01) and heart rate (P < 0.05) was observed after transport, as compared to before loading values (pre-transport). No differences between basal I, basal II and before loading values (pre-transport) for physiological parameters were observed.
The highest T3, T4 and fT4 levels recorded after short transport seem to suggest a preferential release from the thyroid gland. The results indicate that short road transport stress contributes significantly to thyroid hormone changes, according to different breed, and to the increase in rectal temperature and heart rate. No differences related to different age were observed. |
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Department of Morphology, Biochemistry, Physiology and Animal Production – Unit of Veterinary Physiology, Faculty of Veterinary Medicine, University of Messina, Polo Universitario Annunziata, 98168 Messina, Italy |
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Corporate Author |
Cravana, C. |
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IESM 2008 |
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Poster IESM 2008 |
Approved |
yes |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4494 |
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