Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase

Particulate cell fractions of mycelium of Mucor rouxii contain adenylate cyclase activity which can be partially solubilized by 0.5 m KCl. Homogenates prepared in the presence of Lubrol PX or KCl exhibit two- to threefold more activity compared to homogenates prepared in the absence of detergent or...

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Autor principal:	Cantore de Ezcurra, María Leonor
Publicado:	1982
Materias:	adenylate cyclase article cell fractionation enzymology isolation and purification kinetics metabolism Mucor solubility Adenylate Cyclase Kinetics Solubility Subcellular Fractions Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v219_n1_p1_Cantore http://hdl.handle.net/20.500.12110/paper_00039861_v219_n1_p1_Cantore
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00039861_v219_n1_p1_Cantore
record_format	dspace
spelling	paper:paper_00039861_v219_n1_p1_Cantore2023-06-08T14:25:00Z Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase Cantore de Ezcurra, María Leonor adenylate cyclase article cell fractionation enzymology isolation and purification kinetics metabolism Mucor solubility Adenylate Cyclase Kinetics Mucor Solubility Subcellular Fractions Support, Non-U.S. Gov't Particulate cell fractions of mycelium of Mucor rouxii contain adenylate cyclase activity which can be partially solubilized by 0.5 m KCl. Homogenates prepared in the presence of Lubrol PX or KCl exhibit two- to threefold more activity compared to homogenates prepared in the absence of detergent or salt. The membrane-bound enzyme prepared in the presence of 2% Lubrol PX was studied in detail. The kinetic properties of this adenylate cyclase were as expected for an allosteric enzyme with the ATP · Mn2- complex as substrate and free Mn2+ ions as activator. Unchelated ATP inhibits the reaction by competing with the substrate. The KCl-solubilized enzyme was partially purified by ion-exchange chromatography, ammonium sulfate precipitation, and gel filtration. Molecular parameters of the solubilized enzyme are: Stokes radius, 8.6 nm; S20,w, 13S; Mr 510,000; and frictional ratio, 1.60. © 1982. Fil:Cantore, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1982 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v219_n1_p1_Cantore http://hdl.handle.net/20.500.12110/paper_00039861_v219_n1_p1_Cantore
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 article cell fractionation enzymology isolation and purification kinetics metabolism Mucor solubility Adenylate Cyclase Kinetics Mucor Solubility Subcellular Fractions Support, Non-U.S. Gov't
spellingShingle	adenylate cyclase article cell fractionation enzymology isolation and purification kinetics metabolism Mucor solubility Adenylate Cyclase Kinetics Mucor Solubility Subcellular Fractions Support, Non-U.S. Gov't Cantore de Ezcurra, María Leonor Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase
topic_facet	adenylate cyclase article cell fractionation enzymology isolation and purification kinetics metabolism Mucor solubility Adenylate Cyclase Kinetics Mucor Solubility Subcellular Fractions Support, Non-U.S. Gov't
description	Particulate cell fractions of mycelium of Mucor rouxii contain adenylate cyclase activity which can be partially solubilized by 0.5 m KCl. Homogenates prepared in the presence of Lubrol PX or KCl exhibit two- to threefold more activity compared to homogenates prepared in the absence of detergent or salt. The membrane-bound enzyme prepared in the presence of 2% Lubrol PX was studied in detail. The kinetic properties of this adenylate cyclase were as expected for an allosteric enzyme with the ATP · Mn2- complex as substrate and free Mn2+ ions as activator. Unchelated ATP inhibits the reaction by competing with the substrate. The KCl-solubilized enzyme was partially purified by ion-exchange chromatography, ammonium sulfate precipitation, and gel filtration. Molecular parameters of the solubilized enzyme are: Stokes radius, 8.6 nm; S20,w, 13S; Mr 510,000; and frictional ratio, 1.60. © 1982.
author	Cantore de Ezcurra, María Leonor
author_facet	Cantore de Ezcurra, María Leonor
author_sort	Cantore de Ezcurra, María Leonor
title	Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase
title_short	Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase
title_full	Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase
title_fullStr	Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase
title_full_unstemmed	Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase
title_sort	kinetic properties, solubilization, and molecular characterization of mucor rouxii adenylate cyclase
publishDate	1982
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v219_n1_p1_Cantore http://hdl.handle.net/20.500.12110/paper_00039861_v219_n1_p1_Cantore
work_keys_str_mv	AT cantoredeezcurramarialeonor kineticpropertiessolubilizationandmolecularcharacterizationofmucorrouxiiadenylatecyclase
_version_	1768541824395247616

Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase

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