{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T10:46:24Z","timestamp":1774781184287,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1999,4,1]]},"abstract":"<jats:p>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\u2013 and BeF3\u2013). 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.<\/jats:p>","DOI":"10.1023\/a:1020154325630","type":"journal-article","created":{"date-parts":[[2003,3,15]],"date-time":"2003-03-15T13:36:10Z","timestamp":1047735370000},"page":"81-87","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Fluorimetric Analysis of Phospholipase Activity in <i>Tetrahymena pyriformis GL<\/i>."],"prefix":"10.1042","volume":"19","author":[{"given":"P\u00e9ter","family":"Kov\u00e1cs","sequence":"first","affiliation":[{"name":"Department of Genetics, Cell and Immunobiology, Semmelweis University of Medicine, H-1445, Budapest, POB 370, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gy\u00f6rgy","family":"Csaba","sequence":"additional","affiliation":[{"name":"Department of Genetics, Cell and Immunobiology, Semmelweis University of Medicine, H-1445, Budapest, POB 370, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Bioscience Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/bioscirep\/article-pdf\/19\/2\/81\/470054\/bsr0190081.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/bioscirep\/article-pdf\/19\/2\/81\/470054\/bsr0190081.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,16]],"date-time":"2021-11-16T17:48:47Z","timestamp":1637084927000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/bioscirep\/article\/19\/2\/81\/54173\/Fluorimetric-Analysis-of-Phospholipase-Activity-in"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,4,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1999,4,1]]}},"URL":"https:\/\/doi.org\/10.1023\/a:1020154325630","relation":{},"ISSN":["0144-8463","1573-4935"],"issn-type":[{"value":"0144-8463","type":"print"},{"value":"1573-4935","type":"electronic"}],"subject":[],"published":{"date-parts":[[1999,4,1]]}}}