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Structural assignment and extractability of microsomal estradiol receptors.
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
|September 1, 1983
Summary
Estradiol receptor extraction from porcine endometrium microsomes is enhanced by Surfynol and dithiothreitol. Enzymes like trypsin further increase yields, suggesting different receptor forms in cellular membranes.
Area of Science:
- Endocrinology and Reproductive Biology
- Molecular and Cellular Biology
Background:
- Estradiol receptors play a crucial role in reproductive processes.
- Understanding receptor extraction is key to studying their function.
Purpose of the Study:
- To optimize the extraction of estradiol receptor forms from porcine endometrium.
- To investigate the effects of various agents on receptor solubilization and yield.
Main Methods:
- Extraction of estradiol receptor from crude porcine endometrium microsomes using low ionic strength buffers.
- Assessment of yield improvements with Surfynol 485 and dithiothreitol.
- Enzymatic treatment with trypsin and hyaluronoglucosaminidase to evaluate effects on receptor forms.
Main Results:
- Surfynol 485 and dithiothreitol significantly increase estradiol receptor yields (3-4 fold).
- Trypsin dramatically enhances yields and modifies receptor structure, while hyaluronoglucosaminidase converts acidic to basic forms.
- Distinct acidic and basic receptor distributions are observed in smooth and rough endoplasmic reticulum fractions.
Conclusions:
- Combined use of Surfynol and dithiothreitol is highly effective for estradiol receptor extraction.
- Enzymatic treatments offer further yield enhancement and insights into receptor heterogeneity.
- Subcellular localization of receptor forms correlates with enzyme efficacy.