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 beta-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.
Highlights
Of Sanger et al [8];both M13 primers and synthetic oligonucleotide primers were used in the sequencing
Sequencing of ApoB-100 Peptides-LDL was purified from the plasma of a patient with familial heterozygous type I1 hyperlipoproteinemia [9]
Baylor College of Medicine and The Methodist Hospital, mixture was fractionated on a 2.6 X 150-cm Sephadex G-50 column
Summary
We have determined the complete sequence of apolipoprotein (apo) B-100 cDNA. We identified 2366 residues of apoB-100 by direct sequence analysis of apoB-100 tryptic peptides. The mature peptide contains 2 5 cysteine residues, 12 of which are in the N-terminal
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