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

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Abstract

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
Volume74
Issue number4
DOIs
StatePublished - Feb 21 1977

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LDL Lipoproteins
Glass
Lymphocytes
LDL Receptors
Fibroblasts
Ionic strength
Osmolar Concentration
Lipoproteins
Albumins
Membranes
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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title = "Specific, saturable, and high affinity binding of 125I-low density lipoprotein to glass beads",
abstract = "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.",
author = "Dana, {Suzanna E.} and Brown, {Michael S.} and Goldstein, {Joseph L.}",
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T1 - Specific, saturable, and high affinity binding of 125I-low density lipoprotein to glass beads

AU - Dana, Suzanna E.

AU - Brown, Michael S.

AU - Goldstein, Joseph L.

PY - 1977/2/21

Y1 - 1977/2/21

N2 - 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.

AB - 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.

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