Lipophilic proteins of Friend erythroleukemia cells

Abstract

Lipophilic proteins can be extracted from Friend mouse erythroleukemia cells (MELC) with acidic chloroform-methanol. The acidic extract contains at least 4 polypeptides of apparent M.W. 5, 9, 5, 14 and 17 kdaltons as determined by SDS-polyacrylamide gel electrophoresis (PAGE). Delipidation of the extract with ether causes the formation of polymers of an apparent molecular weight ranging from 25 to 85 kdaltons, and strong binding of aminoacids, sugars and phospholipids, in particular phosphatidylinositol and phosphatidylethanolamine, to the polypeptides. Through the majority of the lipophilic proteins are of cellular origin, part of the polypeptides of M.W. 14 and 17 kdaltons may be viral components.