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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Autores principales: Cantore, M.L., Passeron, S.
Formato: JOUR
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: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 todo:paper_00039861_v219_n1_p1_Cantore
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spelling todo:paper_00039861_v219_n1_p1_Cantore2023-10-03T13:56:58Z Kinetic properties, solubilization, and molecular characterization of Mucor rouxii adenylate cyclase Cantore, M.L. Passeron, S. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, M.L.
Passeron, S.
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.
format JOUR
author Cantore, M.L.
Passeron, S.
author_facet Cantore, M.L.
Passeron, S.
author_sort Cantore, M.L.
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
url http://hdl.handle.net/20.500.12110/paper_00039861_v219_n1_p1_Cantore
work_keys_str_mv AT cantoreml kineticpropertiessolubilizationandmolecularcharacterizationofmucorrouxiiadenylatecyclase
AT passerons kineticpropertiessolubilizationandmolecularcharacterizationofmucorrouxiiadenylatecyclase
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