The unicellular Tetrahymena enzymatically split the synthetic phosphodiester, 4-methylum-belliferyl phosphocoline substrate. The enzyme activity was completely blocked in vitro and drastically inhibited in vivo by G-protein activating fluorides (NaF; AlF4– and BeF3–). The phospholipase A2 inhibitor, quinacrine, and the protein phosphatase inhibitor, neomycin, inhibited the enzyme activity in vitro and activated it in vivo. Another phospholipase A2 inhibitor 4-bromo phenacyl bromide was ineffective in vivo and in vitro alike, as well as the cyclooxygenase inhibitor indomethacin. Results of these experiments indicate that some treatments could be specific for a well defined activity (e.g., phospholipase A2, G-protein) but subject to influence by other enzymes (e.g., phospholipase C, sphingomyelinase). The experiments call attention to the differences in the results of the in vivo and in vitro studies.
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Research Article| April 01 1999
Fluorimetric Analysis of Phospholipase Activity in Tetrahymena pyriformis GL.
Biosci Rep (1999) 19 (2): 81–87.
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Péter Kovács, György Csaba; Fluorimetric Analysis of Phospholipase Activity in Tetrahymena pyriformis GL.. Biosci Rep 1 April 1999; 19 (2): 81–87. doi: https://doi.org/10.1023/A:1020154325630
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