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Bovine cerebellum endothelin receptor: solubilization and identification
I Schvartz1, O Ittoop, E Hazum
1Division of Endocrinology, Glaxo Research Laboratories, Research Triangle Park, North Carolina 27709.
Endocrinology
|June 1, 1990
Summary
Bovine cerebellum endothelin receptors were successfully solubilized using CHAPS detergent, retaining high affinity binding. Identification of a 50-kD protein band suggests it represents the endothelin receptor.
Area of Science:
- Neuroscience
- Biochemistry
- Pharmacology
Background:
- Endothelin receptors play crucial roles in various physiological processes.
- Understanding receptor characteristics is vital for pharmacological research.
Purpose of the Study:
- To solubilize and characterize endothelin receptors from bovine cerebellum.
- To identify the molecular weight of the endothelin receptor.
Main Methods:
- Solubilization of membrane preparations using CHAPS detergent.
- Binding assays to determine affinity and receptor density.
- Affinity chromatography and iodination for protein identification.
- SDS-PAGE and autoradiography to determine molecular weight.
Main Results:
- Endothelin receptors were solubilized in an active form with high affinity (Kd = 7 ± 2 nM) and saturability.
- Binding characteristics were preserved post-solubilization.
- A 50-kD protein band was identified as the putative endothelin receptor.
Conclusions:
- CHAPS effectively solubilizes active endothelin receptors from bovine cerebellum.
- The 50-kD protein identified is likely the endothelin receptor, preserving binding properties.