0000000000455317

AUTHOR

Isabelle Bourdil

showing 2 related works from this author

Active vanadate-sensitive H+ translocation in corn roots membrane vesicles and proteoliposomes

1988

Abstract A member fraction from corn roots which contains a vanadate-sensitive ATPase activity has been prepared. The specific activity at 38°C is between 3 and mol 12 μmol · min −1 · mg −1 , depending on the age of roots. Addition of ATP promotes a very rapid quenching of the fluorescence of 9-amino-6-chloro-3-methoxy-acridin (ACMA). Proton pumping exhibits a delayed sensitivity to vanadate but is strongly and instantaneously inhibited by the new inhibitor SW 26. Both proton pumping, measured by the initial quenching rate, and ATP hydrolysis show maximum activities at ATP concentrations in the millimolar range, but the apparent K m -value for hydrolysis is higher than that observed for pro…

0106 biological sciencesTrisMolar concentrationATPase[SDV]Life Sciences [q-bio]Plant Science01 natural sciences03 medical and health scienceschemistry.chemical_compoundHydrolysisATP hydrolysisProton transportGeneticsVanadateComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesQuenching (fluorescence)biologyGeneral Medicine[SDV] Life Sciences [q-bio]chemistryBiochemistrybiology.proteinBiophysicsAgronomy and Crop Science010606 plant biology & botany
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Cercospora beticola Toxin Inhibits Vanadate-Sensitive H+ Transport in Corn Root Membrane Vesicles

1988

The effect of Cercospora beticola toxin on the transport of protons by vanadate-sensitive ATPase was studied with corn (Zea mays) root microsomal vesicles prepared by differential centrifugation, sedimentation through a sucrose cushion, and washing with Triton X-100 plus KBr. In these preparations, addition of ATP induced intravesicular H(+)-accumulation as evidenced by a rapid quenching of the fluorescence of 9-amino-6-chloro-2-methoxy acridine. This quenching was relatively unaffected by inhibitors of mitochondrial and tonoplast-type ATPases, but was strongly reduced by inhibitors of plasma membrane H(+)-ATPase. C. beticola toxin markedly inhibited ATP dependent H(+)-transport, and this e…

0106 biological sciencesPhysiology[SDV]Life Sciences [q-bio]ATPasePlant Sciencemedicine.disease_cause01 natural sciences03 medical and health sciencesGeneticsmedicineVanadateMembranes and BioenergeticsCERCOSPORA BETICULAComputingMilieux_MISCELLANEOUS030304 developmental biologyDifferential centrifugation0303 health sciencesQuenching (fluorescence)biologyToxinVesicleMembrane transportCercospora beticolabiology.organism_classification[SDV] Life Sciences [q-bio]Biochemistrybiology.protein010606 plant biology & botanyPlant Physiology
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