Specific, saturable, and high affinity binding of 125I-low density lipoprotein to glass beads

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


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 languageEnglish (US)
Pages (from-to)1369-1376
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Feb 21 1977

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Specific, saturable, and high affinity binding of <sup>125</sup>I-low density lipoprotein to glass beads'. Together they form a unique fingerprint.

Cite this