Structure of apolipoprotein C-IIToronto, a nonfunctional human apolipoprotein

Proc Natl Acad Sci U S A. 1987 Jan;84(1):270-3. doi: 10.1073/pnas.84.1.270.

Abstract

We previously reported a family with apolipoprotein C-II (apoC-II) deficiency characterized by the presence of a mutant apoC-II, apoC-IIToronto. We now report the purification and primary structure of apoC-IIToronto. The sequence of apoC-IIToronto is identical to that of normal apoC-II from residues 1-68. It differs from residue 69, where Asp69-Gln70-Val71-Leu72-Ser73-Val74- Leu75-Lys76-Gly77-Glu78-Glu79 is replaced by Thr69-Lys70-Phe71-Phe72-Leu73-Cys74. This is consistent with the deletion of a nucleotide in the codon for either Thr68 or Asp69 and a translation reading frame shift.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Apolipoprotein C-II
  • Apolipoproteins C / blood*
  • Apolipoproteins C / isolation & purification
  • Chromatography, High Pressure Liquid
  • Humans
  • Mutation*
  • Peptide Fragments / analysis

Substances

  • Amino Acids
  • Apolipoprotein C-II
  • Apolipoproteins C
  • Peptide Fragments
  • apolipoprotein C-II (Toronto)