Journal of Lipid Research, Vol. 9, 627-635, September 1968
Copyright © 1968 by Lipid Research, Inc.
Effect of phospholipase A treatment of low density lipoproteins on the dextran sulfate-lipoprotein interaction
Toshiro Nishida
The Burnsides Research Laboratory, University of Illinois, Urbana, Illinois 61801
The effect of phospholipase A on the interaction of low density lipoproteins of the Sf 0-10 class with dextran sulfate was studied in phosphate buffer of pH 7.4, ionic strength 0.1, by chemical, spectrophotometric, and centrifugal methods. When low density lipoproteins that had been treated with phospholipase A were substituted for untreated lipoproteins, the amount of insoluble dextran sulfate-lipoprotein complex formed was greatly reduced. Hydrolysis of over 20% of the lecithin and phosphatidyl ethanolamine constituents of the lipoproteins prevented the formation of insoluble complex. However, even the lipoproteins in which almost all the phosphoglycerides were hydrolyzed produced soluble complex, which was converted to insoluble complex upon addition of magnesium sulfate. It is apparent that the lipoproteins altered extensively by treatment with phospholipase A retain many characteristic properties of native low density lipoproteins.
Fatty acids, but not lysolecithin, released by the action of phospholipase A interfered with the formation of insoluble complex; this interference was due to association of the fatty acids with the lipoproteins. With increases in the concentration of the associated fatty acids, the amounts of magnesium ion required for the conversion of soluble complex to insoluble complex increased progressively. Charge interaction is evidently of paramount importance in the formation of sulfated polysaccharide-lipoprotein complexes.
Supplementary key words phospholipase A • low density lipoproteins • dextran sulfate • insoluble complex • soluble complex • fatty acids • magnesium ion • lysolecithin • albumin
Submitted on March 14, 1968
Accepted on June 19, 1968
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