Biochemical effects of luxabendazole on Trichinella spiralis
Identifieur interne : 003084 ( Main/Exploration ); précédent : 003083; suivant : 003085Biochemical effects of luxabendazole on Trichinella spiralis
Auteurs : A. Criado-Fornelio [Espagne] ; C. De Armas-Serra [Espagne] ; A. Jimenez-Gonzalez [Espagne] ; N. Casado-Escribano [Espagne] ; F. Rodriguez-Caabeiro [Espagne]Source :
- Parasitology Research [ 0932-0113 ] ; 1990-06-01.
English descriptors
- Teeft :
- Anthelmintic, Ascaris suum, Assay, Biochemical effects, Colchicine, Colchicine binding, Free glucose, Fumarate reductase activity, Glucose, Glucose uptake, Glycogen, Glycogen contents, Glycogen levels, Glycogen reserves, Larva, Luxabendazole, Microtubule, Microtubule protein, Mitochondrial fraction, Other benzimidazoles, Parasitol, Present study, Previous work, Protein contents, Reductase, Spiralis, Standard pepsin digestion, Succinate dehydrogenase, Trichinella spiralis, Tubulin, Vivo treatment.
Abstract
Abstract: Biochemical changes produced by luxabendazole in muscle-stageTrichinella spiralis larvae consisted of a decrease in free glucose and glycogen levels (46.71% and 35.66%, respectively) after in vivo treatment, slight in vitro inhibition of fumarate reductase activity (24.15%) and, finally, inhibition of [3H]-colchicine-tubulin binding, which was found to be of a competitive nature, with an inhibition constant (Ki) of 0.9×10−7 M. In a parallel study, luxabendazole did not appear to be inhibitory to [3H]-colchicine binding to pig-brain tubulin.
Url:
DOI: 10.1007/BF00931057
Affiliations:
Links toward previous steps (curation, corpus...)
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Le document en format XML
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<term>Glycogen contents</term>
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<front><div type="abstract" xml:lang="en">Abstract: Biochemical changes produced by luxabendazole in muscle-stageTrichinella spiralis larvae consisted of a decrease in free glucose and glycogen levels (46.71% and 35.66%, respectively) after in vivo treatment, slight in vitro inhibition of fumarate reductase activity (24.15%) and, finally, inhibition of [3H]-colchicine-tubulin binding, which was found to be of a competitive nature, with an inhibition constant (Ki) of 0.9×10−7 M. In a parallel study, luxabendazole did not appear to be inhibitory to [3H]-colchicine binding to pig-brain tubulin.</div>
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