Biochimica et Biophysica Acta (BBA) - Biomembranes
Regular paperRapid purification and reconstitution of a plant vacuolar ATPase using Triton X-114 fractionation: Subunit composition and substrate kinetics of the H+-ATPase from the tonoplast of Kalanchoë daigremontiana
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Cited by (24)
Three-dimensional map of a plant V-ATPase based on electron microscopy
2002, Journal of Biological ChemistryCitation Excerpt :The K. daigremontiana V-ATPase samples used in our analysis by electron microscopy were characterized for purity and activity by SDS-PAGE and activity assays, respectively. Fig. 1A shows the typical polypeptide pattern of the V-ATPase after purification that corresponded to what has been reported previously (23, 33). During recent work the D-subunit (34 kDa) and two E-subunit isoforms (32 and 33 kDa) have been identified in the K. daigremontianaV-ATPase by matrix-assisted laser desorption ionization-mass spectroscopy (34).
Structure, function and regulation of the plant vacuolar H<sup>+</sup>-translocating ATPase
2000, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Km values ranging from 200 to 810 μM have been reported for different plant V-ATPases [34,62,65–69]. For the substrate hydrolysis activity of the K. daigremontiana V-ATPase two Km values (770 μM and 2 μM) have been found [70], indicating the presence of at least two different catalytic centers at the enzyme or cooperativity between nucleotide binding sites. By relating nitrate-sensitive V-ATPase activity to immunologically determined V-ATPase protein amount in tonoplast vesicles isolated from Me.
The Physiology, Biochemistry and Molecular Biology of the Plant Vacuolar ATPase
1997, Advances in Botanical ResearchFunctional reconstitution of the tonoplast proton-ATPase from higher plants
1997, International Review of Cytology
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Present address: Department of Plant Sciences, University of Oxford, South Park Road, Oxford OX1 3RB, UK.