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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Kornblihtt, A.R., Flawiá, M.M., de Mendoza, D., Glikin, G., Farías, R., Torres, H.N.
Formato: JOUR
Materias:
adenylate cyclase
liothyronine
animal experiment
male genital system
rat
testis
Adenylate Cyclase
Animals
Cytosol
Kinetics
Male
Protein Binding
Rats
Seminiferous Tubules
Testis
Triiodothyronine
Animalia
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03008177_v36_n1_p23_Kornblihtt
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
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.

Ejemplares similares