Search results for "Manduca sexta"

showing 6 items of 16 documents

Purification and reassessment of ligand binding by the recombinant, putative juvenile hormone receptor of the tobacco hornworm, Manduca sexta

1996

The 29 kDa protein from the larval epidermis of the tobacco hornworm, Manduca sexta, that specifically bound photoaffinity analogs of JH I and JH II was produced by a recombinant baculovirus (rJP29). The higher of the two molecular weight forms made corresponded to a protein that could be formed by read‐through of the TGA termination codon to the following TAA. The previously reported, apparent high affinity binding of [methyl‐3H]‐JH I by rJP29 as measured by the dextran‐coated charcoal (DCC) assay [Palli et al., Proc Natl Acad Sci USA 91:6191–6195 (1994)] was found to be artifactual due to endogenous cellular esterases that co‐purified with rJP29 through both DEAE cellulose and MonoQ chrom…

Manduca sextaTn5 cellsjuvenile hormone receptorcellular esterasesSf21 cellsrecombinant baculovirus proteinJH esterasephotoaffinity labelingArchives of Insect Biochemistry and Physiology
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Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
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Hypoxia and anoxia in insects: microcalorimetric studies on two species (Locusta migratoria and Manduca sexta) showing different degrees of anoxia to…

1995

Abstract Microcalorimetry was used to study the effects of graded hypoxia and anoxia on two species of insects that differ in their tolerance of anoxia. Locusts (Locusta migratoria) can survive an atmosphere of pure nitrogen for not more than 4 h (at room temperature), whereas hawk moths (Manduca sexta) can recover from more than 24 h of anoxia. To produce graded hypoxia, air and pure nitrogen were mixed and this mixture was passed through the cells of a twin calorimeter equipped with circulation cells. A gas flow containing 2% or more of oxygen had no significant effect on behaviour (as observed in parallel experiments using transparent cells) or heat flow rate. If oxygen content was reduc…

biologyChemistrySphingidaeHypoxia (environmental)chemistry.chemical_elementCondensed Matter Physicsbiology.organism_classificationAnoxic watersOxygenManduca sextaBiophysicsLimiting oxygen concentrationRate of heat flowPhysical and Theoretical ChemistryManducaInstrumentationThermochimica Acta
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Covalent modificaition of juvenile hormone binding proteins by photoaffinity labeling: An unexpected gel shift effect

1994

The 32 kD juvenile hormone binding protein (JHBP) and two 80 kD proteins in larval Manduca sexta hemolymph were labeled with [3H]FDK, a photoaffinity analog of methyl farnesoate (MF). The labeling could be completely displaced by a 30-fold excess of either MF or JH II, demonstrating that [3H]FDK binds specifically to the JH binding sites of the 32 kD JHBP and the 80 kD proteins. In addition, a high molecular-mass protein was labeled with [3H]FDK; labeling could be displaced by excess MF but not by JH II, demonstrating the selectivity in binding MF. The 32 kD JHBP also appeared to weakly bind the potent juvenoid, methoprene, at the JH binding site. Covalent modification by [3H]FDK induced a …

chemistry.chemical_classificationAffinity labelinghemolymphPhotoaffinity labelingPhysiologyBinding proteinmethoprene analogGeneral MedicineBiologyLigand (biochemistry)BiochemistryAmino acidmanduca sextaIsoelectric pointmethyl farnesoatechemistryBiochemistryInsect ScienceJuvenile hormoneJH II analogBinding siteArchives of Insect Biochemistry and Physiology
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Embryonic integument and "molts" in Manduca sexta (Insecta, Lepidoptera).

2002

In Manduca sexta the germ band is formed 12 h post-oviposition (p.o.) (=10% development completed) and is located above the yolk at the egg surface. The cells show a polar organization. They are engaged in the uptake and degradation of yolk globules, pinched off from the yolk cells. This process can be observed in the integumental cells during the first growth phase of the embryo that lasts until “katatrepsis,” an embryonic movement that takes place at 40% development completed. At 37% development completed, the ectoderm deposits a thin membrane at its apical surface, the first embryonic membrane, which detaches immediately before katatrepsis. The second period of embryonic growth—from kata…

food.ingredientCuticleEctodermArthropod cuticleApical cellfoodYolkManducaEctodermmedicineAnimalsPhylogenybiologyfungiEmbryoAnatomybiology.organism_classificationCell biologymedicine.anatomical_structureManduca sextaLarvaAnimal Science and ZoologyIntegumentEpidermisDigestive SystemDevelopmental BiologyJournal of morphology
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Expression and characterization of the recombinant juvenile hormone epoxide hydrolase (JHEH) from Manduca sexta.

1998

The cDNA of the microsomal Juvenile Hormone Epoxide Hydrolase (JHEH) from Manduca sexta was expressed in vitro in the baculovirus system. In insect cell culture, the recombinant enzyme (Ms-JHEH) was produced at a high level (100 fold over background EH catalytic activity). As expected, Ms-JHEH was localized in the microsomal fraction with a molecular mass of approximately 50 kDa. Ms-JHEH showed a substrate and inhibitor spectrum similar to the wild type JHEH isolated from eggs of M. sexta. Its enzymatic activity was the highest for Juvenile Hormone III. Ms-JHEH hydrolyzed several trans-epoxides faster than cis-epoxides. A putative hydroxyl-acyl enzyme intermediate was isolated suggesting a …

mechanismGene ExpressionBiochemistryPolymerase Chain ReactionSubstrate SpecificityManduca sextaManducaHydrolaseAnimalsEpoxide hydrolaserecombinant enzymeMolecular BiologyDNA Primerschemistry.chemical_classificationEpoxide HydrolasesbiologyMolecular massBase Sequencejuvenile hormoneInsect cell cultureHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyRecombinant Proteinsepoxide hydrolaseJuvenile HormonesEnzymechemistryBiochemistryManduca sextaInsect ScienceJuvenile hormoneManducaBaculoviridaeInsect biochemistry and molecular biology
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