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Agonist-specific alterations in receptor binding affinity associated with solubilization of turkey erythrocyte membrane beta adrenergic receptors
L. J. Pike
, R. J. Lefkowitz
Department of Biochemistry & Molecular Biophysics
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
DBBS - Molecular Cell Biology
Research output
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Contribution to journal
›
Article
›
peer-review
43
Scopus citations
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Dive into the research topics of 'Agonist-specific alterations in receptor binding affinity associated with solubilization of turkey erythrocyte membrane beta adrenergic receptors'. Together they form a unique fingerprint.
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Biochemistry, Genetics and Molecular Biology
Agonist
100%
Binding Affinity
100%
Adrenergic Receptor
100%
Erythrocyte Membrane
100%
Turkey (Bird)
100%
Solubilization
100%
Receptor Binding
100%
Binding Site
50%
Stereospecificity
25%
Digitonin
25%
Keyphrases
Turkey
100%
Particulate
100%
Receptor Binding Affinity
100%
β-adrenergic Receptor
100%
Erythrocyte Membrane
100%
Binding Site
33%
Receptor-binding Domain
33%
Molecular Mechanism
33%
High Affinity
33%
Stereospecificity
33%
Digitonin
33%
Immunology and Microbiology
Agonist
100%
Receptor Binding
100%
Binding Affinity
100%
Erythrocyte Membrane
100%
Turkey (Bird)
100%
Solubilization
100%
Binding Site
50%
Stereospecificity
25%
Chemistry
Binding Site
100%
Receptor Binding Affinity
100%
Solubilization
100%
Adrenergic
50%
Digitonin
50%
Pharmacology, Toxicology and Pharmaceutical Science
Turkey (Bird)
100%