Abstract：
:It is shown that conformational changes of receptor proteins brought about by binding of a ligand induce changes in the lipid environment of the receptor that can be monitored by fluorescent lipid probes. On this basis a new approach to studies of ligand-receptor binding is proposed. Using the interaction of the ricin B-chain with Burkitt lymphoma cells as an example and fluorescent labelled sphingomyelin as a probe, the ligand-induced changes of fluorescence anisotropy were shown to be concentration-dependent and to permit determination of the binding constant and the number of receptor-binding sites. The method was found to be specific and highly sensitive, allowing detection of the action of one RB molecule per cell. Scatchard analysis of the binding of 125I-RB demonstrated the presence on the cell surface of two binding sites with Kd approximately 10(-10) and approximately 10(-8) M, respectively. Only the high-affinity sites were detected by the fluorescence technique. Saturation of these sites resulted in maximum inhibition of protein synthesis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Manevich EM,Tonevitsky AG,Bergelson LDdoi
10.1016/0014-5793(86)80108-9subject
Has Abstractpub_date
1986-01-06 00:00:00pages
313-6issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(86)80108-9journal_volume
194pub_type
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