Chemical modification by maleylation of the human plasma high density lipoprotein-protein, apoA-II, causes significant changes in its properties. These changes are as follows: 1) a shift from a helical to a more disordered secondary structure; 2) a decreased ability to bind egg phosphatidylcholine vesicles; and 3) a decrease in immunoreactivity as measured by a quantitative radioimmunoassay. Each of these changes was reversed by demaleylation. These results are discussed in relation to a molecular theory of lipid binding by the plasma lipoproteins.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 23 1974|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology