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, Alberto Rodolfo, Flawiá, Mirtha María, Torres, Héctor Norberto
Publicado:	1981
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:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v20_n5_p1262_Kornblihtt 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	paper:paper_00062960_v20_n5_p1262_Kornblihtt
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spelling	paper:paper_00062960_v20_n5_p1262_Kornblihtt2023-06-08T14:30:37Z Manganese Ion Dependent Adenylate Cyclase Activity in Rat Testes: Purification and Properties Kornblihtt, Alberto Rodolfo Flawiá, Mirtha María Torres, Héctor Norberto 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. 1981 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v20_n5_p1262_Kornblihtt 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, Alberto Rodolfo Flawiá, Mirtha María Torres, Héctor Norberto 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.
author	Kornblihtt, Alberto Rodolfo Flawiá, Mirtha María Torres, Héctor Norberto
author_facet	Kornblihtt, Alberto Rodolfo Flawiá, Mirtha María Torres, Héctor Norberto
author_sort	Kornblihtt, Alberto Rodolfo
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
publishDate	1981
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v20_n5_p1262_Kornblihtt http://hdl.handle.net/20.500.12110/paper_00062960_v20_n5_p1262_Kornblihtt
work_keys_str_mv	AT kornblihttalbertorodolfo manganeseiondependentadenylatecyclaseactivityinrattestespurificationandproperties AT flawiamirthamaria manganeseiondependentadenylatecyclaseactivityinrattestespurificationandproperties AT torreshectornorberto manganeseiondependentadenylatecyclaseactivityinrattestespurificationandproperties
_version_	1768546519459299328

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

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