The primary structure of apolipoprotein A-I from rabbit high-density lipoprotein. Academic Article uri icon

Overview

abstract

  • 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 protease 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 located 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.

publication date

  • October 15, 1986

Research

keywords

  • Apolipoproteins A
  • Metalloendopeptidases

Identity

Scopus Document Identifier

  • 0022990588

Digital Object Identifier (DOI)

  • 10.1111/j.1432-1033.1986.tb09990.x

PubMed ID

  • 3095115

Additional Document Info

volume

  • 160

issue

  • 2