Primary structure of Beijing duck apolipoprotein A-1

Zi Wei Gu, Yong Hong Xie, Manlan Yang, James T. Sparrow, Keqin Wang, You Li, Wen Hsiung Li, Antonio M. Gotto, Chao Yuh Yang

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7 Scopus citations


The primary structure of Beijing duck apolipoprotein A-1 was determined by sequencing peptide fragments derived from tryptic and endoproteinase Asp-N digestion of the protein, and alignment with homologous chicken apo A-1. All of the peptide fragments were isolated by high-pressure liquid chromatography (HPLC) with a Vydac C18 column using a trifluoroacetic acid (TFA) buffer system. The N-terminus of the protein was determined to be aspartic acid by directly sequencing 52 residues of the intact protein. The C-terminus was alanine. The protein contains 240 amino acid residues. By analysis of the whole protein and its tryptic peptides, a six amino acid (Arg-Tyr-Phe-Trp-Gln-His) prosegment was determined. No cross-reactivity between duck and human apo A-1 with a goat antiserum against human apo A-1 was found. Sequence analysis of apo A-1 of other species indicates that amino acid substitutions in rat are more extensive than in other mammals. Isoleucine residues in apo A-1 are inversely correlated to the homology of human to other species, except dog.

Original languageEnglish (US)
Pages (from-to)585-591
Number of pages7
JournalJournal of Protein Chemistry
Issue number5
StatePublished - Oct 1993


  • apo A-1 sequence
  • HDL

ASJC Scopus subject areas

  • Biochemistry


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