Abstract
We have determined the complete sequence of apolipoprotein (apo) B-100 cDNA. It is 14.1 kilobases in length and codes for a 4563-amino acid protein, including a 27-amino acid signal peptide and a 4536-amino acid mature protein. Further, we identified 2366 residues of apoB-100 by direct sequence analysis of apoB-100 tryptic peptides. The mature peptide is characterized by high hydrophobicity (0.916 kcal/residue) and predicted β-sheet content (21%). Dot matrix analysis revealed the presence of many long internal repeats in apoB-100. The mature peptide contains 25 cysteine residues, 12 of which are in the N-terminal 500 residues. Twenty potential N-linked glycosylation sites were identified, of which 13 were proven to be glycosylated, and 4 were found not to be glycosylated by direct analysis of tryptic peptides. Our findings on apoB structure provide a basis for future experimentation on the role of apoB-100 containing lipoproteins in atherosclerosis.
Original language | English (US) |
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Pages (from-to) | 12918-12921 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 261 |
Issue number | 28 |
State | Published - 1986 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology