A new high-yield procedure for the purification of the non-specific phospholipid transfer protein from rat liver.

Rat liver contains a non-specific phospholipid transfer protein that transfers phosphatidylethanolamine, phosphatidylcholine, phosphatidylinositol and sphingomyelin as well as cholesterol between membranes (Bloj, B. and Zilversmit, D.B. (1977) J. Biol. Chem. 252, 1613-1619). The present paper describes a new high-yield procedure for the purification of this protein which includes fractionation on DEAE-cellulose, Sephadex G-50 and hydroxyapatite. Starting from a pH 5.1 supernatant, a homogeneous protein was obtained after a 1 540-fold purification at a yield of 50%. The protein has a molecular weight of 14 800 as estimated by electrophoresis on polyacrylamide gels in the presence of SDS. It has a blocked N-terminal amino acid and a tryptophanyl fluorescence emission maximum at 335 nm. Its amino acid composition has been determined and compared to data published by others on similar proteins.