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Activation of the phospholipase A1 activity of lipoprotein lipase by apoprotein C-II

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Lipids

Abstract

The effect of apo very low density lipoprotein (apo VLDL) and apoprotein C-II on the phospholipase A1 activity associated with lipoprotein lipase (E.C.3.1.1.3) was studied using purified bovine milk lipoprotein lipase. The enzyme degraded14C phosphatidylcholine (PC) to14C 2-acyl lysophosphatidylcholine at a rate of 0.28±0.01 nmol/min/ml and triolein at a rate of 20.3±0.4 nmol/min/ml in mixed emulsions of PC and triolein. The phospholipase activity and triacylglycerol lipase activity were both increased by the addition of apo VLDL and apoprotein C-II. After maximal activation, the rate of PC degradation was 1.19±0.02 nmol/min/ml and triolein degradation 64.4±0.4 nmol/min/ml. Activation of phospholipase A1 activity and triacylglycerol lipase activity occurred in parallel.

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Authors and Affiliations

  1. Lipid Research Laboratory, St. Bartholomew's Hospital, West Smithfield, EC1A 7BE, London, England

    J. Stocks & D. J. Galton

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  1. J. Stocks
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  2. D. J. Galton
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Stocks, J., Galton, D.J. Activation of the phospholipase A1 activity of lipoprotein lipase by apoprotein C-II. Lipids 15, 186–190 (1980). https://doi.org/10.1007/BF02540967

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  • DOI: https://doi.org/10.1007/BF02540967

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