Abstract
Human plasma high density lipoproteins (HDL) were labeled in vitro with [125I]apoA-I. Chromatography of the [125I]HDL on Sephacryl S-200 revealed that a certain fraction of [125I]apoA-I readily dissociates from the intact particle over a wide range of HDL concentrations. The relatively constant value of the dissociated apoA-I concentration observed at various HDL concentrations suggests that a "critical monomer concentration" of apoA-I is in equilibrium with the parent lipoprotein. Addition of [131I]apoC proteins to HDL induces additional dissociation of oligomeric apoA-I with the concomitant incorporation of apoC into a new particle of about 460,000 daltons.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 408-414 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 85 |
| Issue number | 1 |
| DOIs | |
| State | Published - Nov 14 1978 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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