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- W2023759296 abstract "Lipid body membranes purified from castor seed endosperm of dry seeds and 4 d old seedlings were found to have an ATPase activity associated with them. This was confirmed by equilibrium density centrifugation of the membranes using acid lipase as a marker enzyme. The specific activity ranged from 45 to 200 nanomoles per milligram protein per minute. The pH optimum was 9.0 but at pH 7.5 nearly 40% of the maximum activity was retained. The apparent K m for Mg-ATP was 0.5 millimolar. A divalent cation was required for activity and Mg2+ was the most effective. Other nucleoside triphosphates were also hydrolyzed but there was no hydrolysis of pyrophosphate or p-nitrophenylphosphate. The ATPase was not inhibited by oligomycin, vanadate, dicyclohexylcarbodiimide, or molybdate but was inhibited by sodium azide. Washing the membranes with increasing concentrations of NaCl removed up to 60% of the ATPase activity but none was removed by 3 millimolar ethylene-diaminetetraacetate." @default.
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- W2023759296 date "1986-11-01" @default.
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- W2023759296 title "ATPase in Lipid Body Membranes of Castor Bean Endosperm" @default.
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- W2023759296 doi "https://doi.org/10.1104/pp.82.3.671" @default.
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