Determination of the molecular mass of apolipoprotein B-100. A chemical approach

C. Y. Yang, F. S. Lee, L. Chan, D. A. Sparrow, J. T. Sparrow, Antonio Gotto

Research output: Contribution to journalArticle

8 Scopus citations

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 languageEnglish (US)
Pages (from-to)777-780
Number of pages4
JournalBiochemical Journal
Volume239
Issue number3
DOIs
StatePublished - 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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