| Autor: |
C A Reardon, R V Hay, J I Gordon, G S Getz |
| Jazyk: |
angličtina |
| Rok vydání: |
1984 |
| Předmět: |
|
| Zdroj: |
Journal of Lipid Research, Vol 25, Iss 4, Pp 348-360 (1984) |
| Druh dokumentu: |
article |
| ISSN: |
0022-2275 |
| DOI: |
10.1016/S0022-2275(20)37808-1 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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