Primary structure of Beijing duck apolipoprotein A-1.
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.
Gu
Z W
ZW
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030.
Xie
Y H
YH
Yang
M
M
Sparrow
J T
JT
Wang
K
K
Li
Y
Y
Li
W H
WH
Gotto
A M
AM
Yang
C Y
CY
D000595:Amino Acid Sequence; D000818:Animals; D016632:Apolipoprotein A-I / Q000737:chemistry*; D002417:Cattle; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D003429:Cross Reactions; D004285:Dogs; D004372:Ducks / Q000097:blood*; D010450:Endopeptidases; D006801:Humans; D008251:Macaca; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010449:Peptide Mapping; D010802:Phylogeny; D011336:Probability; D017433:Protein Structure, Secondary; D011817:Rabbits; D051381:Rats
D016632:Apolipoprotein A-I; D010446:Peptide Fragments; D010450:Endopeptidases