Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations.
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.
D000262:Adenylyl Cyclases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008297:Male; D011485:Protein Binding; D051381:Rats; D012671:Seminiferous Tubules / Q000201:enzymology*; D013737:Testis / Q000201:enzymology*; D014284:Triiodothyronine / Q000378:metabolism*
D014284:Triiodothyronine; D000262:Adenylyl Cyclases