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.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 18 1972|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology