Abstract
An E-type ecto-ATPase activity was demonstrated in the unicellular eukaryote, Tetrahymena. The in vivo membrane bound activity was increased 4 fold by exposing cells to 50mM NaCl for 1 hour, suggesting its activity can be regulated. It is also released in a soluble form over time. Both forms are recognized by antibodies to the smooth muscle ecto-ATPase of chicken, all with molecular weights of about 66kD. The soluble form was purified over 660 fold and it showed a single 66kD band on SDS-PAGE. This ecto-ATPase only hydrolyzes nucleoside triphosphates but it prefers ATP over GTP by 4 fold. In purinergic reception, GTP is normally more effective as a chemorepellent in these cells than ATP. Their sensitivities were greatly increased by inhibiting nTP hydrolysis. Cells were most sensitive to the non-hydrolyzable analogs (beta-gamma methylene GTP and ATP) at similar concentrations. This suggests that the ecto-ATPase may play a role in sensitivity and selectivity of the purinergic responses of Tetrahymena.
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© 1997 Springer Science+Business Media New York
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Smith, T.M., Kim, M.Y., Kirley, T.L., Hennessey, T.M. (1997). Ecto-ATPase of Tetrahymena. In: Plesner, L., Kirley, T.L., Knowles, A.F. (eds) Ecto-ATPases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5955-9_17
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DOI: https://doi.org/10.1007/978-1-4615-5955-9_17
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