Primary structure of Beijing duck apolipoprotein A-1. Academic Article uri icon

Overview

abstract

  • 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.

publication date

  • October 1, 1993

Research

keywords

  • Apolipoprotein A-I
  • Ducks
  • Protein Structure, Secondary

Identity

Scopus Document Identifier

  • 0027133448

Digital Object Identifier (DOI)

  • 10.1007/BF01025123

PubMed ID

  • 8142001

Additional Document Info

volume

  • 12

issue

  • 5