Journal of Lipid Research, Vol. 8, 46-53, January 1967
Copyright © 1967 by Lipid Research, Inc.

Post-heparin serum lecithinase in man and its positional specificity

William C. Vogel and Edwin L. Bierman

Medical Service, Veterans Administration Hospital and Department of Medicine, University of Washington School of Medicine, Seattle

Lecithinase activity in post-heparin serum has been demonstrated. Phosphatidyl choline (PC) can be degraded to lysophosphatidyl choline and fatty acids at a rate of more than 1 µmole/hr per ml of serum in an incubation system containing PC, 0.1 m glycine-NaOH buffer (pH 9.6), and deoxycholate. This activity cannot be found in serum obtained prior to the injection of heparin.

Post-heparin serum lecithinase can be distinguished from the heat-stable pancreatic lecithinase by the markedly different effects of heat, paraoxon, and EDTA, and from serum lecithin:cholesterol acyltransferase by the differential effect of p-hydroxymercuribenzoate. In contrast to the acyltransferase and to pancreatic lecithinase, which are active at the ßbeta; (C-2) position of lecithin, post-heparin serum lecithinase is active at ' (C-1) position.

Supplementary key words post-heparin serum • man • '-lecithinase • phosphatidyl choline • egg lecithin • cabbage lecithin • lecithin fatty acids • phospholipase

Submitted on May 13, 1966
Accepted on October 3, 1966

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