| Records |
| Author |
Scherer, W.F.; Dickerman, R.W.; Ordonez, J.V. |
| Title |
Discovery and geographic distribution of Venezuelan encephalitis virus in Guatemala, Honduras, and British Honduras during 1965-68, and its possible movement to Central America and Mexico |
Type |
Journal Article |
| Year |
1970 |
Publication |
The American Journal of Tropical Medicine and Hygiene |
Abbreviated Journal |
Am J Trop Med Hyg |
| Volume |
19 |
Issue |
4 |
Pages |
703-711 |
| Keywords |
Animals; Antibodies/analysis; Belize; Central America; Complement Fixation Tests; Cricetinae; Culicidae; *Disease Reservoirs; Ecology; Encephalitis Viruses/isolation & purification; Encephalomyelitis, Equine/*epidemiology; Guatemala; Hemagglutination Inhibition Tests; Honduras; Horses; Humans; Mexico; Neutralization Tests; Rats; Sampling Studies; Swine; Tropical Climate |
| Abstract |
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| Language |
English |
Summary Language |
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Series Title |
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Series Issue |
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Edition |
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| ISSN |
0002-9637 |
ISBN |
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Expedition |
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Conference |
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| Notes |
PMID:4393224 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2735 |
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| Author |
Joubert, L.; Oudar, J.; Hannoun, C.; Beytout, D.; Corniou, B.; Guillon, J.C.; Panthier, R. |
| Title |
[Epidemiology of the West Nile virus: study of a focus in Camargue. IV. Meningo-encephalomyelitis of the horse] |
Type |
Journal Article |
| Year |
1970 |
Publication |
Annales de l'Institut Pasteur |
Abbreviated Journal |
Ann Inst Pasteur (Paris) |
| Volume |
118 |
Issue |
2 |
Pages |
239-247 |
| Keywords |
Animals; Ecology; Encephalitis Viruses/*isolation & purification; Encephalomyelitis, Equine/*epidemiology/immunology; France; Hemagglutination Inhibition Tests; Meningoencephalitis/*veterinary; Neurologic Manifestations; Serologic Tests |
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| Language |
French |
Summary Language |
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Original Title |
Epidemiologie du virus West Nile: etude d'un foyer en Camargue. IV. La meningo-encephalomyelite du cheval |
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Abbreviated Series Title |
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Edition |
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| ISSN |
0020-2444 |
ISBN |
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Expedition |
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Conference |
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| Notes |
PMID:5461277 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2737 |
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| Author |
Mizuguchi, M.; Arai, M.; Ke, Y.; Nitta, K.; Kuwajima, K. |
| Title |
Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy |
Type |
Journal Article |
| Year |
1998 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
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| Volume |
283 |
Issue |
1 |
Pages |
265-277 |
| Keywords |
equine lysozyme; protein folding; molten globule; stopped-flow; folding intermediate |
| Abstract |
The equilibrium unfolding and the kinetics of unfolding and refolding of equine lysozyme, a Ca2+-binding protein, were studied by means of circular dichroism spectra in the far and near-ultraviolet regions. The transition curves of the guanidine hydrochloride-induced unfolding measured at 230 nm and 292.5 nm, and for the apo and holo forms of the protein have shown that the unfolding is well represented by a three-state mechanism in which the molten globule state is populated as a stable intermediate. The molten globule state of this protein is more stable and more native-like than that of α-lactalbumin, a homologous protein of equine lysozyme. The kinetic unfolding and refolding of the protein were induced by concentration jumps of the denaturant and measured by stopped-flow circular dichroism. The observed unfolding and refolding curves both agreed well with a single-exponential function. However, in the kinetic refolding reactions below 3 M guanidine hydrochloride, a burst-phase change in the circular dichroism was present, and the burst-phase intermediate in the kinetic refolding is shown to be identical with the molten globule state observed in the equilibrium unfolding. Under a strongly native condition, virtually all the molecules of equine lysozyme transform the structure from the unfolded state into the molten globule, and the subsequent refolding takes place from the molten globule state. The transition state of folding, which may exist between the molten globule and the native states, was characterized by investigating the guanidine hydrochloride concentration-dependence of the rate constants of refolding and unfolding. More than 80% of the hydrophobic surface of the protein is buried in the transition state, so that it is much closer to the native state than to the molten globule in which only 36% of the surface is buried in the interior of the molecule. It is concluded that all the present results are best explained by a sequential model of protein folding, in which the molten globule state is an obligatory folding intermediate on the pathway of folding. |
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no |
| Call Number |
refbase @ user @ |
Serial |
3990 |
| Permanent link to this record |
