Phosphatidylcholine and phosphatidylinositol exchange proteins in rat liver.

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Abstract
The phospholipid exchange proteins in rat liver that stimulate the transfer of phosphatidylcholine and phosphatidylinositol between membranes were separated into 3 fractions and partially purified by acid pH precipitation, gel filtration on Sephadex G-75, and ion exchange chromatography on DEAE-cellulose and CM-cellulose. Throughout the steps of the purification, both the phosphatidylcholine exchange activity and the phosphatidylinositol exchange activity were measured by a liposome-liposome assay system, which used concanavalin A in the separation of donor and acceptor liposomes. One of the fractions was purified 172-fold and stimulated the phosphatidylcholine exchange but not the phosphatidylinositol exchange. The other 2 fractions were active in the stimulation of the phosphatidylinositol exchange as well as the phosphatidylcholine exchange and were purified 62- and 58-fold over the cell supernatant fraction with respect to the phosphatidylinositol exchange activity. These 2 fractions stimulated the transfer of phosphatidylinositol from donor liposomes to acceptor liposomes initially deficient in this phospholipid.

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