Abstract
A crude membrane preparation isolated from wheat ( Triticum aestivum L. cv. Winalta) roots was separated by differential and sucrose density gradient centrifugation into three fractions which were analysed using sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE). One of these fractions is enriched in nitrate-sensitive ATP ase activity and contains nitrate-sensitive and vanadate-insensitive, ATP-dependent proton-translocating activity. This presumptive tonoplast(TP)-enriched fraction also contains a 68–70-kDa polypeptide which strongly cross-reacts with antiserum developed against an amino-terminus peptide of the 70-kDa subunit of the carrot ( Daucus carota) L. vacuolar ATPase. We have also found that AlF 4 − (fluoroaluminate), a reputed G protein activator, strongly inhibits vanadate-sensitive ATPase activity, but has relatively little effect on the nitrate-sensitive ATPase activity in wheat root membranes.
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