5-Aminolaevulinate hydro-lyase from yeast isolation and purification

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An enzyme, aminolaevulinate dehydratase (5-aminolaevulinate hydro-lyase (adding 5-aminolaevulinate and cyclizing), EC 4.2.1.24), which catalyzes the following reaction: {A figure is presented} has been isolated from yeast. Its purification and some of its properties have been studied. 5-Aminolaevuli...

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Detalles Bibliográficos
Autor principal: Clara de Barreiro, O.L.
Formato: Artículo publishedVersion
Publicado: 1967
Materias:
cellulose
enzyme
Hydro Lyases
hydrolyase
levulinic acid
article
cell membrane
chromatography
electrophoresis
enzymology
freeze drying
kinetics
metabolism
pH
physiology
Saccharomyces
temperature
Cell Membrane
Cellulose
Chromatography
Electrophoresis
Enzymes
Freeze Drying
Hydro-Lyases
Hydrogen-Ion Concentration
Kinetics
Levulinic Acids
Temperature
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v139_n2_p479_ClaradeBarreiro
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v139_n2_p479_ClaradeBarreiro_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
Descripción
Sumario:An enzyme, aminolaevulinate dehydratase (5-aminolaevulinate hydro-lyase (adding 5-aminolaevulinate and cyclizing), EC 4.2.1.24), which catalyzes the following reaction: {A figure is presented} has been isolated from yeast. Its purification and some of its properties have been studied. 5-Aminolaevulinate synthetase, another enzyme involved in porphyrin biosynthesis, has been detected in the mitochondrial particles. © 1967.

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