The primary structure of apolipoprotein A‐I from rabbit high‐density lipoprotein

Chao‐yuh ‐y YANG, Tseming YANG, Henry J. POWNALL, Antonio M. GOTTO

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19 Scopus citations


The amino acid sequence of rabbit apolipoprotein A-I (apo A-I) has been determined by degradation and alignment of two overlapping sets of peptides obtained from tryptic and staphylococcal digestions. All of the peptides of rabbit apo A-I resulting from digestion by staphylococcal preotease were isolated and sequenced except residues 33-37. A digestion with trypsin was employed to find overlapping and missing peptides. The N-terminus of rabbit apo A-I was confirmed by sequencing the intact protein up to 20 residues while the C-terminus was identified through its homology with human apo A-I. The protein contains 241 residues in its single chain. Its primary structure is highly homologous to the reported canine apo A-I (80%) and human apo A-I (78%), but exhibits less similarity with rat apo A-I (60%). Like human apo A-I, rabbit apo A-I contains very little histidine (2) and methionine (1); it does however have two residues of isoleucine. Based on a comparison of the hydrophobic-hydrophilic character of apo A-I residues with that of the two synthetic peptides that activated lecithin:cholesterol acyltransferase (Pownall et al. and Yokoyama et al.), we found that the five segments with the highest corresponding homologies on the protein are lcoated within the N-terminal half. This suggests that the N-terminal half of apo A-I contains the major portion of regions activating lecithin:cholesterol acyltransferase.

Original languageEnglish (US)
Pages (from-to)427-431
Number of pages5
JournalEuropean Journal of Biochemistry
Issue number2
StatePublished - Oct 1986

ASJC Scopus subject areas

  • Biochemistry


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