A method to measure receptor binding of ligands with low affinity. Application to plasma proteins binding assay with hemopoietic cells

Levesque, JP, Hatzfeld, A and Hatzfeld, J (1985) A method to measure receptor binding of ligands with low affinity. Application to plasma proteins binding assay with hemopoietic cells. Experimental Cell Research, 156 2: 558-562. doi:10.1016/0014-4827(85)90563-4


Author Levesque, JP
Hatzfeld, A
Hatzfeld, J
Title A method to measure receptor binding of ligands with low affinity. Application to plasma proteins binding assay with hemopoietic cells
Journal name Experimental Cell Research   Check publisher's open access policy
ISSN 0014-4827
Publication date 1985-01-01
Sub-type Article (original research)
DOI 10.1016/0014-4827(85)90563-4
Volume 156
Issue 2
Start page 558
End page 562
Total pages 5
Language eng
Subject 1307 Cell Biology
Abstract A gradient has been developed for separating free ligand from ligand bound to cells growing in suspension. This method can be used with all kinds of ligand but it is particularly useful for those ligands having the tiresome tendency to adhere to the cells non-specifically or to polymerize by themselves. This is the case of fibronectin, fibrinogen, immunoglobulins and many other plasma proteins. The gradient consists of two layers: an upper aqueous phase and a lower hydrophobic organic phase. The aqueous phase, a sucrose buffer, allows the cells to become well dispersed before they enter the hydrophobic phase which excludes the free ligand efficiently. This reduces non-specific binding and allows the accurate measurement of specific binding which could not be obtained with a gradient made of a single phase. Depending upon the size and the density of the cells, and the nature of the ligand, the assay method can be modified by changing the density or the nature of the hydrophilic and hydrophobic phases.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
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Citation counts: TR Web of Science Citation Count  Cited 12 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 9 times in Scopus Article | Citations
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