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.
Skip Nav Destination
Article navigation
Research Article|
April 01 1999
Fluorimetric Analysis of Phospholipase Activity in Tetrahymena pyriformis GL.
Péter Kovács;
Péter Kovács
1Department of Genetics, Cell and Immunobiology, Semmelweis University of Medicine, H-1445, Budapest, POB 370, Hungary
Search for other works by this author on:
György Csaba
György Csaba
1Department of Genetics, Cell and Immunobiology, Semmelweis University of Medicine, H-1445, Budapest, POB 370, Hungary
Search for other works by this author on:
Publisher: Portland Press Ltd
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1999 Plenum Publishing Corporation
1999
Biosci Rep (1999) 19 (2): 81–87.
Citation
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
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Cited By
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() |