Density gradient localization of vanadate- and NO-3-sensitive ATPase from sterile cultures of Spirodela polyrrhiza (L.) Schleiden

Józef Buczek, Jadwiga Sulej


The present work deals with the separation and some characteristics of ATPase activities bound with plant membanes prepared from sterile cultures of Spirodela polyrrhiza. The membrane-bound ATPases were separated on sucrose gradients and distinguished by membrane density and sensitivity to several inhibitors. The results showed that N0-3-sensitive ATPase activity associated with the tonoplast was localized at a sucrose density between 1.095-1.117 g•cm-3. The vanadate-sensitive ATPase activity bound with the plasma membrane showed a density between 1.127-1.151 g•cm-3. Both ATPases were insensitive to azide and oligomycin and were separable from markers for mitochondria.


Spirodela polyrrhiza (L.) Schleiden; membrane-bound ATPase

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