Abstract
By circular dichroic, fluorescence and ultracentrifugal methods, it is shown that apoLP-alanine binds to dimyristoyl phosphatidylcholine in its liquid crystalline state more efficiently than its gel state.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 779-786 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 60 |
| Issue number | 2 |
| DOIs | |
| State | Published - Sep 23 1974 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Fingerprint
Dive into the research topics of 'The requirement for lipid fluidity in the formation and structure of lipoproteins: Thermotropic analysis of apolipoprotein-alanine binding to dimyristoyl phosphatidylcholine'. Together they form a unique fingerprint.Cite this
- APA
- Standard
- Harvard
- Vancouver
- Author
- BIBTEX
- RIS