ATPase of basal bodies of Tetrahymena pyriformis.

The Ca2+-ATPase activity in basal bodies of Tetrahymena pyriformis was determined by cytochemical and biochemical methods. It was found that the sites of the Ca2+-ATPase activity are associated with the basal body microtubules. A method for the isolation of the basal bodies in a purified form in amounts for biochemical assay has been developed.

[Extraction and investigation of ATPase of Tetrahymena pyriformis cilia].

The ATPase-active proteins were solubilized from T. pyriformis of cilia by treatment of the cilia with the non-ionic detergent Triton X-100. The activity of Triton-solubilized ATPase is stimulated by Ca2+ and is sensitive to EGTA.

[Mimosa pudica adenosine triphosphatase].

The morphological structure (pulvinus P1, P2 and P3) directly involved in the seismonastic movements of the Mimosa pudica leaf have been used to isolate: 1) "soluble" ATPase, loosely bound to pulvinus structures; 2) Ca, Mg-dependent ATPase, which is tightly bound to pulvinus structures and is extracted by a saline solution of high ionic strength, used to isolate actomyosin from muscles and non-muscle motile cells; 3) ATPase bound to the pulvinus membrane structures, which is solubilized by the detergents, e. g. Triton X-100 and Tween-80, and is similar to membrane ATPase.