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Platelet activating factor‐acetylhydrolase in insects: Identification and partial characterization of a 1‐alkyl‐2‐acetyl‐ sn ‐glycero‐3‐phosphocholine acetylhydrolase in a cell‐free system of Heliothis
Author(s) -
Lambremont Edward N.,
Malone Boyd,
Snyder Fred
Publication year - 1988
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940070105
Subject(s) - biology , biochemistry , phosphocholine , platelet activating factor , phospholipase a2 , dithiothreitol , phosphatidylcholine , phospholipid , egta , moiety , phospholipase a1 , phospholipase , acyl group , calcium , alkyl , enzyme , stereochemistry , chemistry , organic chemistry , membrane , immunology
A specific acetylhydrolase that inactivates platelet activating factor (PAF; 1‐alkyl‐2‐acetyl‐sn‐glycero‐3‐phosphocholine), a potent cellular mediator in mammalian cells, by removal of the sn ‐2 acetyl moiety, has been found in the cytosolic fraction of several postembryonic developmental stages and specific tissues of the corn earworm, Heliothis zea (Boddie). Effects of magnesium, calcium, EGTA, deoxycholate, dithiothreitol, diisopropylfluorophosphate, egg phosphatidylcholine, and an acylacetyl‐glycerophosphocholine show that hydrolysis of the acetate moiety is due to a specific acetylhydrolase for PAF. The activity does not appear to be due to a typical cellular phospholipase A 2 that utilizes phospholipid substrates with a long‐chain acyl group at position sn ‐2 of glycerol. Specific activities and properties of the acetylhydrolase from this insect match closely with those described from tissues of vertebrate animals.