Isolation of a helical, lipid-binding fragment from the human plasma high density lipoprotein, apolp-GLN-I Academic Article Article uri icon

Overview

MeSH Major

  • Obesity
  • Thinness
  • Weight Gain

abstract

  • The major apolipoprotein of human plasma high density lipoproteins (HDL), apoLP-Gln-I, has previously been shown to have a high content of α-helical conformation and a molecular weight of approximately 28,000. Our results show that apoLP-Gln-I contains three methionine residues. We have treated apoLP-Gln-I with cyanogen bromide (CNBr) and have isolated the four CNBr fragments by chromatography on BioGel P-30. One of the fragments, CNBr-I has 92 amino acid residues, contains no homoserine or methionine and corresponds to the carboxyl-terminal peptide. This fragment is of particular interest since it was shown to retain a high content of α-helix, while the other fragments were mainly disordered, and to possess the ability to bind phosphatidyl choline. © 1972.

publication date

  • December 18, 1972

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0006-291X(72)90501-3

PubMed ID

  • 4344811

Additional Document Info

start page

  • 1444

end page

  • 51

volume

  • 49

number

  • 6