Summary
Cytosolic adenylate cyclase activity from rat seminiferous tubules was purified by chromatography 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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Kornblihtt, A.R., Flawiá, M.M., de Mendoza, D. et al. Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations. Mol Cell Biochem 36, 23–27 (1981). https://doi.org/10.1007/BF02354828
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DOI: https://doi.org/10.1007/BF02354828