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Author |
Scherer, W.F.; Madalengoitia, J.; Flores, W.; Acosta, M. |
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Title |
Ecologic studies of Venezuelan encephalitis virus in Peru during 1970-1971 |
Type |
Journal Article |
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Year |
1975 |
Publication |
American Journal of Epidemiology |
Abbreviated Journal |
Am J Epidemiol |
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Volume |
101 |
Issue |
4 |
Pages |
347-355 |
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Keywords |
Animals; Antibodies, Viral; Cricetinae/immunology; Culicidae/microbiology; *Disease Vectors; Ecology; *Encephalitis Virus, Venezuelan Equine/immunology/isolation & purification; Encephalomyelitis, Equine/immunology/microbiology/transmission; Female; Hemagglutination Inhibition Tests; Horses/immunology; Humans; Neutralization Tests; Peru |
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Abstract |
Venezuelan encephalitis (VE) virus has intermittently produced epidemics and equine epizootics on the dry Pacific coastal plain of Peru since at least the 1930's. However, evidence that the virus exists in the Amazon region of Peru to the east of the Andes mountains was not obtained until antibodies were found in human sera collected in 1965, and 10 strains of the virus were isolated in a forest near the city of Iquitos, Peru during February and March 1971. Eight strains came from mosquitoes and two from dead sentinel hamsters. Three hamsters exposed in forests near Iquitos developed VE virus antibodies suggesting that hamster-benign strains also exist there. Antibody tests of equine sera revealed no evidence that VE virus was actively cycling during the late 1950's or 1960's in southern coastal Peru, where equine epizootics had occurred in the 1930's and 1940's. In northern coastal Peru bordering Ecuador, antibodies were present in equine sera, presumably residual from the 1969 outbreak caused by subtype I virus, since neutralizing antibody titers were higher to subtype I virus than to subtypes III or IV. No VE virus was detected in this northern region during the dry season of 1970 by use of sentinel hamsters. The possibility is considered that VE epidemics and equine epizootics on the Pacific coast of Peru are caused by movements of virus in infected vertebrates traversing Andean passes or in infected vertebrates or mosquitoes carried in airplanes from the Amazon region. |
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0002-9262 |
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PMID:235838 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2705 |
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Author |
Dunn, M.F.; Branlant, G. |
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Title |
Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation |
Type |
Journal Article |
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Year |
1975 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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Volume |
14 |
Issue |
14 |
Pages |
3176-3182 |
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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 |
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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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0006-2960 |
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Notes |
PMID:238585 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3817 |
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Author |
Nelson, W.A.; Keirans, J.E.; Bell, J.F.; Clifford, C.M. |
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Title |
Host-ectoparasite relationships |
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Journal Article |
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Year |
1975 |
Publication |
Journal of Medical Entomology |
Abbreviated Journal |
J Med Entomol |
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Volume |
12 |
Issue |
2 |
Pages |
143-166 |
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Keywords |
Animal Nutrition Physiology; Animals; Anoplura/physiology; *Arthropods; Birds/parasitology; Chickens/parasitology; Dermacentor/parasitology; Diptera; Ecology; Feeding Behavior; Female; Horses/parasitology; Humans; Male; Mallophaga/physiology; Mice/parasitology; Mites/physiology; Reproduction; Sarcoptes scabiei/physiology; Sheep/parasitology; Skin/parasitology; Ticks/physiology; Toxins, Biological/toxicity; Trombiculidae/physiology |
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English |
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0022-2585 |
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PMID:808617 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2704 |
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Author |
Makarov, V.V.; Bakulov, I.A. |
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Title |
[Zoopathogenic arboviruses, their systematics and ecology] |
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Journal Article |
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Year |
1975 |
Publication |
Veterinariia |
Abbreviated Journal |
Veterinariia |
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11 |
Pages |
39-41 |
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Animals; Arboviruses/*classification/pathogenicity; Cattle; Deer; Ecology; Horses; Insect Vectors; Sheep; Swine; Turkeys; Viruses/*classification/pathogenicity |
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Russian |
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Zoopatogennye arbovirusy--sistematika i ekologiia |
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ISSN |
0042-4846 |
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Notes |
PMID:814685 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2703 |
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Author |
Czerlinski, G.H.; Wagner, M.; Erickson, J.O.; Theorell, H. |
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Title |
Chemical relaxation studies on the system liver alcohol dehydrogenase, NADH and imidazole |
Type |
Journal Article |
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Year |
1975 |
Publication |
Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry |
Abbreviated Journal |
Acta Chem Scand B |
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Volume |
29 |
Issue |
8 |
Pages |
797-810 |
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Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Computers; Hydrogen-Ion Concentration; Imidazoles/*metabolism; Kinetics; Liver/enzymology/*metabolism; Mathematics; Models, Chemical; NAD/*metabolism; Time Factors |
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Abstract |
Several years ago, Theorell and Czerlinski conducted experiments on the system of horse liver alcohol dehydrogenase, reduced nicotinamide adenine dinucleotide and imidazole, using the first version of the temperature jump apparatus with detection of changes in fluorescence. These early experiments were repeated with improved instrumentation and confirmed the early experiments in general terms. However, the improved detection system allowed to measure a slight concentration dependence of the relaxation time of around 3 ms. Furthermore, the chemical relaxation time was smaller than the one determined earlier (by factor 2). The data were evaluated much more rigorously than before, allowing an appropriate interpretation of the results. The observed relaxation time is largely due to rate constants in an interconversion of ternary complexes, which are faster than three (of the four) dissociation rate constants, determined previously by Theorell and McKinley-McKee.1,2 This fact contributed to earlier difficulties of finding any concentration dependence. However, the binding of imidazole to the binary enzyme-coenzyme complex can be made to couple kinetically into the interconversion rate of the two ternary complexes. The observed signal derives largely from the ternary complex(es). A substantial fluorescence signal change is associated with the observed relaxation process, suggesting a relocation of the imidazole in reference to the nicotinamide moiety of the bound coenzyme. Nine models are considered with two types of coupling of pre-equilibria (none-all). Quantitative evaluations favor the model with two ternary complexes connected by an interconversion outside the four-step (bimolecular) cycle. The ternary complex outside the cycle has much higher fluorescence yield than the one inside. The interconversion equilibrium is near unity for imidazole. If it would be shifted very much to the side of the “dead-end” complex (as in isobutyramide?!), stimulating action could not take place. |
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0302-4369 |
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PMID:882 |
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Call Number |
refbase @ user @ |
Serial |
3887 |
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