J. Lipid Res.
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Journal of Lipid Research, Vol 25, 348-360, Copyright © 1984 by Lipid Research, Inc.

ARTICLES

Processing of rat liver apoprotein E primary translation product

CA Reardon, RV Hay, JI Gordon and GS Getz

The primary translation product of rat liver apoE mRNA was isolated from wheat germ cell-free translation systems. Plasma apoE and the primary translation product migrated similarly on SDS-polyacrylamide gels, had similar partial proteolytic peptide maps, and bound to and coeluted from heparin-Sepharose columns. Comparison of the partial amino acid sequence of the primary translation product with the amino- terminal sequence of plasma apoE indicated that rat apoE is initially synthesized with an 18 amino acid amino-terminal extension. This entire segment was removed cotranslationally by canine microsomes possessing signal peptidase activity. The microsome-processed translation product did not contain an endoglycosidase H-sensitive oligosaccharide, suggesting that rat apoE is O-glycosylated.
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Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.