The primary structure of human apolipoprotein A-IV

Chao yuh Yang, Zi Wei Gu, Ilsong Chong, Weijun Xiong, Maryvonne Rosseneu, Hui xin Yang, Bo rong Lee, Antonio Gotto, Lawrence Chan

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


Human apolipoprotein (apo) A-IV was purified from chylous ascites fluid. Proteolytic peptides produced by trypsin and Staphylococcus aureus V8 proteinase digestions were purified by high-performance liquid chromatography and sequenced. Human apoA-IV contains 376 amino acid residues. The peptide-derived sequence generally matches two previously reported DNA-derived amino acid sequences except for discrepancies in five positions. In order to examine these discrepancies further, one complete apoA-IV cDNA clone and another partial clone were sequenced. Comparison of all the available information indicates that the peptide-derived sequence reported here is accurate. Sequencing errors probably account for some of the discrepancies between the two primary sequences predicted by earlier nucleotide analyses. In certain positions, however, bona fide sequence heterogeneity or cloning artifact cannot be excluded.

Original languageEnglish (US)
Pages (from-to)231-237
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Issue number2
StatePublished - Apr 3 1989


  • Amino acid sequence
  • Apolipoprotein A-IV
  • DNA sequence
  • HDL
  • Lecithin-cholesterol acyltransferase
  • Sequence heterogeneity

ASJC Scopus subject areas

  • Endocrinology
  • Biophysics
  • Biochemistry


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