125I-Low density lipoprotein (125I-LDL)* binds tightly to glass beads at physiologic pH and ionic strength. This binding shows saturability, high affinity (half maximal binding achieved at 10-15 μg protein/ml), and specificity (unlabeled LDL but not HDL or albumin competes with 125I-LDL for binding to the glass beads). In contrast to the binding of 125I-LDL to the physiologic LDL receptor on the surface of human fibroblasts and lymphocytes, the binding of 125I-LDL to bind to inert substances such as glass must be considered in the interpretation of studies in which 125I-LDL binding to membrane receptors is measured. The data emphasize the importance of correlating observed 125I-LDL binding with a physiologic action of the lipoprotein.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Feb 21 1977|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology