Positional Specificity of Phosphatide Acyl Hydrolase (Phospholipase A )

SNAKE venom phospholipase A was shown by de Haas and van Deenen to release the fatty acid constituent present in the β-ester position of mixed-acid phospholipids obtained by a synthesis de novo 1–3 . This result confirmed those of Tattrie 4 and Hanahan et al. 5 , who worked on fatty acid distributio...

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Bibliographic Details
Published in:Nature (London) 1962-10, Vol.196 (4849), p.68-68
Main Authors: HAAS, G. H. DE, DAEMEN, F. J. M, DEENEN, L. L. M. VAN
Format: Article
Language:English
Subjects:
Humanities and Social Sciences
Hydrolases
letter
multidisciplinary
Old Medline
Phosphatidylethanolamines
Phospholipases
Phospholipids
Science
Science (multidisciplinary)
Sensitivity and Specificity
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Summary:SNAKE venom phospholipase A was shown by de Haas and van Deenen to release the fatty acid constituent present in the β-ester position of mixed-acid phospholipids obtained by a synthesis de novo 1–3 . This result confirmed those of Tattrie 4 and Hanahan et al. 5 , who worked on fatty acid distribution in egg lecithin, using phospholipase A , phospholipase D and pancreatic lipase. Hence, the positional specificity of phospholipase A appeared to be settled. Recently Bennett and Tattrie 6 , however, reported, because of reacylation investigations of snake-venom-formed lysolecithin, that this enzyme may not invariably hydrolyse the β-fatty acid ester bonds. This assumption supports the interpretation previously made by Marinetti et al. 7 , indicating a preference of the enzyme for liberating long-chain poly-unsaturated fatty acids, irrespective of their position in the phospholipid molecule. For this reason further investigations into the mode of action of phospholipase A were made.
ISSN:0028-0836
1476-4687
DOI:10.1038/196068a0