Effects of maleylation on the lipid-binding and immunochemical properties of human plasma high density apolipoprotein-A-II

Richard L. Jackson, Simon J.T. Mao, Antonio Gotto

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)1317-1324
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume61
Issue number4
DOIs
StatePublished - Dec 23 1974

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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