Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations

Abstract

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.

DOI: 10.1007/BF02354828

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Cite this paper

@article{Kornblihtt1981AssociationOT, title={Association of triiodothyronine binding activity to soluble adenylate cyclase in testicular preparations}, author={Alberto R . Kornblihtt and Mirtha M. Flawi{\'a} and Diego de Mendoza and Gerardo Claudio Glikin and Raquel Farias and H{\'e}ctor Torres}, journal={Molecular and Cellular Biochemistry}, year={1981}, volume={36}, pages={23-27} }