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Biochemistry
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滴定 ELISA 法测定受体配体相互作用的离解常数
JoVE Journal
Biochemistry
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JoVE Journal
Biochemistry
Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
Please note that all translations are automatically generated.
Click here for the English version.
滴定 ELISA 法测定受体配体相互作用的离解常数
DOI:
10.3791/57334-v
•
12:38 min
•
February 15, 2018
•
Johannes A. Eble
1
Institute of Physiological Chemistry and Pathobiochemistry
,
University of Münster
Chapters
00:04
Title
00:45
Immobilization of the Receptor (Integrin α2A-domain) to a Microtiter Plate
02:09
Preparation of a Serial Dilution Row of the Ligand (Rhodocetin)
03:25
Binding of Ligand at Different Concentrations to Immobilized Receptor
05:03
Quantification of Receptor-bound Ligand by ELISA
07:06
Evaluation of the Titration Signals
09:30
Results: Rhodocetin Binds with Lower Affinity to Mutant Integrin α2A-domain
10:58
Conclusion
Summary
Automatic Translation
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描述了执行滴定 ELISA 的详细协议。此外, 提出了一种新的评价滴定 ELISAs 的方法, 并获得了可溶性配体对微量滴定板固定化受体的离解常数。
Tags
Titration ELISA
Dissociation Constant
Receptor-ligand Interaction
Integrin Alpha 2 A Domain
Rhodocetin
Affinity Constant
Protein-ligand Interaction
Receptor Research
Pharmaceutical Research
Pharmacology
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