Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties

Testicular, soluble adenylate cyclase has been purified by anion-exchange chromatography, gel filtration, and isoelectric focusing. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peak fractions from the latter purification step showed only one polypeptide band with an apparent molec...

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Detalles Bibliográficos
Autores principales: Kornblihtt, A.R., Flawia, M.M., Torres, H.N.
Formato: JOUR
Materias:
adenylate cyclase
manganese
animal
article
enzymology
isolation and purification
male
metabolism
molecular weight
protein conformation
rat
testis
Adenylate Cyclase
Animal
Male
Manganese
Molecular Weight
Protein Conformation
Rats
Support, Non-U.S. Gov't
Testis
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v20_n5_p1262_Kornblihtt
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Testicular, soluble adenylate cyclase has been purified by anion-exchange chromatography, gel filtration, and isoelectric focusing. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peak fractions from the latter purification step showed only one polypeptide band with an apparent molecular weight of about 69 000. The following hydrodynamic and molecular parameters have been established for this enzyme: sedimentation constant, 4.3 S; Stokes radius, 3.95 nm; partial specific volume, 0.74 mL.g-1; molecular weight, 74000; frictional ratio, 1.4. © 1981, American Chemical Society. All rights reserved.

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