Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations
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 bindin...
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Autores principales: | , , , , |
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1981
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v36_n1_p23_Kornblihtt http://hdl.handle.net/20.500.12110/paper_03008177_v36_n1_p23_Kornblihtt |
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Sumario: | 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. © 1981 Martinus Nijhoff/Dr W. Junk Publishers. |
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