title: Purification of the 28 kD Protein from Maize Pollen and Studies on Its Properties.
abstract: A novel protein with ATPase activity was purified from the cytoplasmic extracts of maize pollen by acetone precipitation, ammonium sulfate fractionation, followed by DEAE-Sephadex A(50) and Mono S ion-exchange chromatography. The molecular weight was about 28 kD as determined by SDS-PAGE and the isoelectric point was pH 8.3 by IEF-PAGE. Western blotting analysis showed the 28 kD protein had no specific immuno-reactions with the anti-kinesin monoclonal or the anti-dynamin polyclonal antibodies. The maximum ultraviolet absorbance was at 278 nm, CD spectrum analysis showed the that 28 kD protein with the feature of a globulin. Pharmacological studies indicated that the enzyme activity was strongly inhibited by Na(3)VO(4) but insensitive to NEM. It was inhibited about 50% by NaF. Oligomycin, KNO(3) and ouabain had no effects on its ATPase activity.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, China.
authors.forename: Jian-Hua
authors.initials: JH
authors.lastname: Wang
authors.forename: Ying-Jie
authors.initials: YJ
authors.lastname: Wu
authors.forename: Xian-Rong
authors.initials: XR
authors.lastname: Wu