Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations
- PMID: 7242527
- DOI: 10.1007/BF02354828
Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations
Abstract
Cytosolic adenylate cyclase activity from rat seminiferous tubules was purified by chromtography in DEAE-cellulose, hydroxylapatite and Bio-Gel A-0.5 m as well as by centrifugation in sucrose gradients. In all these purification steps, fractions with adenylate cyclase activity also contained binding activity for L-T3. Binding studies indicate the existence of two L-T3 receptor components associated to adenylate cyclase activity. The component exhibiting the highest hormone affinity has the lowest binding capacity.
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