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
id todo:paper_00062960_v20_n5_p1262_Kornblihtt
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spelling todo:paper_00062960_v20_n5_p1262_Kornblihtt2023-10-03T14:04:20Z Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties Kornblihtt, A.R. Flawia, M.M. Torres, H.N. 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 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. Fil:Kornblihtt, A.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Flawia, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v20_n5_p1262_Kornblihtt
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 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
spellingShingle 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
Kornblihtt, A.R.
Flawia, M.M.
Torres, H.N.
Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties
topic_facet 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
description 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.
format JOUR
author Kornblihtt, A.R.
Flawia, M.M.
Torres, H.N.
author_facet Kornblihtt, A.R.
Flawia, M.M.
Torres, H.N.
author_sort Kornblihtt, A.R.
title Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties
title_short Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties
title_full Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties
title_fullStr Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties
title_full_unstemmed Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties
title_sort manganese ion dependent adenylate cyclase activity in rat testes: purification and properties
url http://hdl.handle.net/20.500.12110/paper_00062960_v20_n5_p1262_Kornblihtt
work_keys_str_mv AT kornblihttar manganeseiondependentadenylatecyclaseactivityinrattestespurificationandproperties
AT flawiamm manganeseiondependentadenylatecyclaseactivityinrattestespurificationandproperties
AT torreshn manganeseiondependentadenylatecyclaseactivityinrattestespurificationandproperties
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