Abstract
Apolipoprotein B-100 (apo B-100) is the protein ligand in low-density lipoproteins that binds to a specific cell-surface receptor. Its molecular mass has been a subject of controversy. We have determined the molecular mass of the protein by a chemical approach. After complete CNBr cleavage, the C-terminal fragment of apo B-100 was purified by reverse-phase h.p.l.c. Amino acid N- and C-terminal analyses confirm that this peptide represents the C-terminal peptide as deduced from the DNA sequence of a human apo B-100 cDNA clone. A chemically synthesized peptide was used to determine the recovery of the peptide (74.72%). On the basis of these data, the molecular mass of apo B-100 was determined to be 496.82 ± 24.84 kDa.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 777-780 |
| Number of pages | 4 |
| Journal | Biochemical Journal |
| Volume | 239 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1986 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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