Journal of Lipid Research, Vol. 5, 177-183, April 1964
Copyright © 1964 by Lipid Research, Inc.

Post-heparin phospholipase

William C. Vogel and Leslie Zieve

Laboratory for Cancer Research, Radioisotope Service and Department of Medicine, Minneapolis Veterans Hospital, University of Minnesota, Minneapolis, Minnesota

Egg phosphatidyl ethanolamine is degraded to lysophosphatidyl ethanolamine and fatty acids by a phospholipase in post-heparin plasma at rates of 10 to 30 µmoles/hr per ml plasma. The optimal system for measuring this enzyme contained albumin and (NH₄)₂SO₄, and the optimal pH was 8.8-9.1. Only slight degradation of egg or beef lecithin occurred.

Post-heparin and pancreatic phospholipase differ in heat stability; in the inhibiting effects of EDTA, HgCl₂, and diethyl-p-nitrophenyl phosphate; in the requirement for deoxycholate or albumin; and in an apparent specificity of the post-heparin enzyme for the ethanolamine phosphatide.

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