The complete cDNA and amino acid sequence of human apolipoprotein B-100

S. H. Chen, C. Y. Yang, P. F. Chen, D. Setzer, M. Tanimura, W. H. Li, A. M. Gotto, L. Chan

Research output: Contribution to journalArticlepeer-review

169 Scopus citations


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 languageEnglish (US)
Pages (from-to)12918-12921
Number of pages4
JournalJournal of Biological Chemistry
Issue number28
StatePublished - 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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