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Author Yamada, T.; Rojanasuphot, S.; Takagi, M.; Wungkobkiat, S.; Hirota, T.
Title Studies on an epidemic of Japanese encephalitis in the northern region of Thailand in 1969 and 1970 Type Journal Article
Year 1971 Publication Biken Journal Abbreviated Journal (up) Biken J
Volume 14 Issue 3 Pages 267-296
Keywords Adolescent; Adult; Animals; Arboviruses/immunology; Buffaloes; Cattle; Chickens; Child; Child, Preschool; Cross Reactions; Culicidae; Dengue Virus/immunology; Disease Outbreaks; Ducks; Ecology; Encephalitis Virus, Japanese/immunology/isolation & purification; Encephalitis, Japanese/cerebrospinal fluid/*epidemiology/immunology/microbiology/mortality; Female; Hemagglutination Inhibition Tests; Hemorrhagic Fevers, Viral/epidemiology; Horses; Humans; Infant; Male; Mice; Neutralization Tests; Swine; Thailand
Abstract
Address
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Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-2324 ISBN Medium
Area Expedition Conference
Notes PMID:4400462 Approved no
Call Number Equine Behaviour @ team @ Serial 2728
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Author Hirota, S.; Suzuki, M.; Watanabe, Y.
Title Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c Type Journal Article
Year 2004 Publication Biochemical and Biophysical Research Communications Abbreviated Journal (up) Biochem Biophys Res Commun
Volume 314 Issue 2 Pages 452-458
Keywords Amino Acids/chemistry; Animals; Cytochromes c/*chemistry; Heme/*chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium/chemistry; Peptides/chemistry; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine/*analogs & derivatives/*chemistry
Abstract Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient absorption spectrum during folding decreased its intensity and red-shifted from 397 to 400 nm by interaction with trityrosine, whereas tyrosinol caused no significant effect. The change in the transient absorption spectrum by interaction with trityrosine was similar to that obtained with 100 mM imidazole, which showed that the population of the intermediate His/His coordinated species increased during folding of cyt c by interaction with trityrosine. The absorption change was biphasic, the fast phase (82+/-9s(-1)) corresponding to the transition from the His/H(2)O to the His/Met coordinated species, whereas the slow phase (24+/-3s(-1)) from His/His to His/Met. By addition of trityrosine, the relative ratio of the slow phase increased, due to increase of the His/His species at the initial stage of folding. According to the resonance Raman spectra of cyt c, the high-spin 6-coordinate and low-spin 6-coordinate species were dominated at pH 2.3 and 4.2, respectively, and these species were not affected by addition of trityrosine. These results demonstrated that the His/His species increased by interaction with trityrosine at the initial stage of cyt c folding, whereas the heme coordination structure was not affected by trityrosine when the protein was completely unfolded or folded. Hydrophobic peptides thus may be useful to study the effects of hydrophobic interactions on protein folding.
Address Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-291X ISBN Medium
Area Expedition Conference
Notes PMID:14733927 Approved no
Call Number Equine Behaviour @ team @ Serial 3777
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Author Bayley, P.; Martin, S.; Anson, M.
Title Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution Type Journal Article
Year 1975 Publication Biochemical and Biophysical Research Communications Abbreviated Journal (up) Biochem Biophys Res Commun
Volume 66 Issue 1 Pages 303-308
Keywords *Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors
Abstract
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-291X ISBN Medium
Area Expedition Conference
Notes PMID:1172440 Approved no
Call Number Equine Behaviour @ team @ Serial 3816
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Author Alexander, F.; Nicholson, J.D.
Title The blood and saliva clearances of phenobarbitone and pentobarbitone in the horse Type Journal Article
Year 1968 Publication Biochemical pharmacology Abbreviated Journal (up) Biochem Pharmacol
Volume 17 Issue 2 Pages 203-210
Keywords Animals; Female; *Horses; Injections, Intravenous; Male; Metabolic Clearance Rate; Pentobarbital/blood/*metabolism; Phenobarbital/blood/*metabolism; Protein Binding; *Saliva; Time Factors
Abstract
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-2952 ISBN Medium
Area Expedition Conference
Notes PMID:5647047 Approved no
Call Number refbase @ user @ Serial 117
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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 (up) 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
Abstract
Address
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
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ISSN 0006-2952 ISBN Medium
Area Expedition Conference
Notes PMID:6053598 Approved no
Call Number refbase @ user @ Serial 118
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Author Polverini, E.; Cugini, G.; Annoni, F.; Abbruzzetti, S.; Viappiani, C.; Gensch, T.
Title Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red Type Journal Article
Year 2006 Publication Biochemistry Abbreviated Journal (up) Biochemistry
Volume 45 Issue 16 Pages 5111-5121
Keywords Animals; Apoproteins/*chemistry/*metabolism; Binding Sites; Computer Simulation; Fluorescent Dyes/analysis; Horses; Hydrogen-Ion Concentration; Models, Molecular; Myoglobin/*chemistry/*metabolism; Oxazines/*analysis/chemistry; Protein Binding; Protein Folding; Protein Structure, Tertiary
Abstract The interaction of nile red (NR) with apomyoglobin (ApoMb) in the native (pH 7) and molten globule (pH 4) states was investigated using experimental and computational methods. NR binds to hydrophobic locations in ApoMb with higher affinity (K(d) = 25 +/- 5 microM) in the native state than in the molten globule state (K(d) = 52 +/- 5 microM). In the molten globule state, NR is located in a more hydrophobic environment. The dye does not bind to the holoprotein, suggesting that the binding site is located at the heme pocket. In addition to monitoring steady-state properties, the fluorescence emission of NR is capable of tracking submillisecond, time-resolved structural rearrangements of the protein, induced by a nanosecond pH jump. Molecular dynamics simulations were run on ApoMb at neutral pH and at pH 4. The structure obtained for the molten globule state is consistent with the experimentally available structural data. The docking of NR with the crystal structure shows that the ligand binds into the binding pocket of the heme group, with an orientation bringing the planar ring system of NR to overlap with the position of two of the heme porphyrin rings in Mb. The docking of NR with the ApoMb structure at pH 4 shows that the dye binds to the heme pocket with a slightly less favorable binding energy, in keeping with the experimental K(d) value. Under these conditions, NR is positioned in a different orientation, reaching a more hydrophobic environment in agreement with the spectroscopic data.
Address Dipartimento di Fisica, Universita degli Studi di Parma, Viale G. P. Usberti 7/A, 43100 Parma, Italy
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:16618100 Approved no
Call Number Equine Behaviour @ team @ Serial 3763
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Author Haruta, N.; Kitagawa, T.
Title Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin Type Journal Article
Year 2002 Publication Biochemistry Abbreviated Journal (up) Biochemistry
Volume 41 Issue 21 Pages 6595-6604
Keywords Animals; Apoproteins/*chemistry; Circular Dichroism; Holoenzymes/chemistry; Horses; Hydrochloric Acid/chemistry; Hydrogen-Ion Concentration; Imidazoles/chemistry; Kinetics; Models, Molecular; Myoglobin/*chemistry; Peptide Fragments/chemistry; *Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman/*methods; Tryptophan/*chemistry; Ultraviolet Rays; Whales
Abstract The 244-nm excited transient UV resonance Raman spectra are observed for the refolding intermediates of horse apomyoglobin (h-apoMb) with a newly constructed mixed flow cell system, and the results are interpreted on the basis of the spectra observed for the equilibrium acid unfolding of the same protein. The dead time of mixing, which was determined with the appearance of UV Raman bands of imidazolium upon mixing of imidazole with acid, was 150 micros under the flow rate that was adopted. The pH-jump experiments of h-apoMb from pH 2.2 to 5.6 conducted with this device demonstrated the presence of three folding intermediates. On the basis of the analysis of W3 and W7 bands of Trp7 and Trp14, the first intermediate, formed before 250 micros, involved incorporation of Trp14 into the alpha-helix from a random coil. The frequency shift of the W3 band of Trp14 observed for this process was reproduced with a model peptide of the A helix when it forms the alpha-helix. In the second intermediate, formed around 1 ms after the start of refolding, the surroundings of both Trp7 and Trp14 were significantly hydrophobic, suggesting the formation of the hydrophobic core. In the third intermediate appearing around 3 ms, the hydrophobicity was relaxed to the same level as that of the pH 4 equilibrium intermediate, which was investigated in detail with the stationary state technique. The change from the third intermediate to the native state needs more time than 40 ms, while the appearance of the native spectrum after the mixing of the same solutions was confirmed separately.
Address School of Mathematical and Physical Sciences, The Graduate University for Advanced Studies, Myodaiji, Okazaki 444-8585, Japan
Corporate Author Thesis
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
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ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:12022863 Approved no
Call Number Equine Behaviour @ team @ Serial 3785
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Author Gulotta, M.; Gilmanshin, R.; Buscher, T.C.; Callender, R.H.; Dyer, R.B.
Title Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape Type Journal Article
Year 2001 Publication Biochemistry Abbreviated Journal (up) Biochemistry
Volume 40 Issue 17 Pages 5137-5143
Keywords Animals; Apoproteins/*chemistry; Computer Simulation; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; *Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence/instrumentation/methods; Thermodynamics; Tryptophan/chemistry
Abstract An acid-destabilized form of apomyoglobin, the so-called E state, consists of a set of heterogeneous structures that are all characterized by a stable hydrophobic core composed of 30-40 residues at the intersection of the A, G, and H helices of the protein, with little other secondary structure and no other tertiary structure. Relaxation kinetics studies were carried out to characterize the dynamics of core melting and formation in this protein. The unfolding and/or refolding response is induced by a laser-induced temperature jump between the folded and unfolded forms of E, and structural changes are monitored using the infrared amide I' absorbance at 1648-1651 cm(-1) that reports on the formation of solvent-protected, native-like helix in the core and by fluorescence emission changes from apomyoglobin's Trp14, a measure of burial of the indole group of this residue. The fluorescence kinetics data are monoexponential with a relaxation time of 14 micros. However, infrared kinetics data are best fit to a biexponential function with relaxation times of 14 and 59 micros. These relaxation times are very fast, close to the limits placed on folding reactions by diffusion. The 14 micros relaxation time is weakly temperature dependent and thus represents a pathway that is energetically downhill. The appearance of this relaxation time in both the fluorescence and infrared measurements indicates that this folding event proceeds by a concomitant formation of compact secondary and tertiary structures. The 59 micros relaxation time is much more strongly temperature dependent and has no fluorescence counterpart, indicating an activated process with a large energy barrier wherein nonspecific hydrophobic interactions between helix A and the G and H helices cause some helix burial but Trp14 remains solvent exposed. These results are best fit by a multiple-pathway kinetic model when U collapses to form the various folded core structures of E. Thus, the results suggest very robust dynamics for core formation involving multiple folding pathways and provide significant insight into the primary processes of protein folding.
Address Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA
Corporate Author Thesis
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ISSN 0006-2960 ISBN Medium
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Notes PMID:11318635 Approved no
Call Number Equine Behaviour @ team @ Serial 3789
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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 (up) 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.
Address
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Language English Summary Language Original Title
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ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:6261802 Approved no
Call Number Equine Behaviour @ team @ Serial 3809
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Author Dunn, M.F.; Branlant, G.
Title Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation Type Journal Article
Year 1975 Publication Biochemistry Abbreviated Journal (up) Biochemistry
Volume 14 Issue 14 Pages 3176-3182
Keywords *Alcohol Oxidoreductases/metabolism; Aldehydes/*pharmacology; Animals; Binding Sites; Enzyme Activation/drug effects; Horses; Hydrogen-Ion Concentration; Kinetics; Liver/enzymology; *NAD/analogs & derivatives/pharmacology; Oxidation-Reduction; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; *Zinc/pharmacology
Abstract 1,4,5,6-Tetrahydronicotinamide adenine dinucleotide (H2NADH) has been investigated as a reduced coenzyme analog in the reaction between trans-4-N,N-dimethylaminocinnamaldehyde (I) (lambdamax 398 nm, epsilonmax 3.15 X 10-4 M-minus 1 cm-minus 1) and the horse liver alcohol dehydrogenase-NADH complex. These equilibrium binding and temperature-jump kinetic studies establish the following. (i) Substitution of H2NADH for NADH limits reaction to the reversible formation of a new chromophoric species, lambdamax 468 nm, epsilonmax 5.8 x 10-4 M-minus 1 cm-minus 1. This chromophore is demonstrated to be structurally analogous to the transient intermediate formed during the reaction of I with the enzyme-NADH complex [Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882]. (ii) The process of intermediate formation with the enzyme-NADH complex is independent of pH over the range 6.13-10.54. Although studies were limited to the pH range 5.98-8.72, a similar pH independence appears to hold for the H2NADH system. (iii) Within the ternary complex, I is bound within van der Waal's contact distance of the coenzyme nicotinamide ring. (iv) Formation of the transient intermediate does not involve covalent modification of coenzyme. Based on these findings, we conclude that zinc ion has a Lewis acid function in facilitating the chemical activation of the aldehyde carbonyl for reduction, and that reduced coenzyme plays a noncovalent effector role in this substrate activating step.
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Language English Summary Language Original Title
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ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:238585 Approved no
Call Number Equine Behaviour @ team @ Serial 3817
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