Porphyrin biosynthesis-immobilized enzymes and ligands-X. A novel approach to the study of the relationship between the quaternary structure of aminolaevulinate dehydratase and its activity

1. 1. Evidence for dissociation, renaturation, re-association and re-hybridization of bovine liver aminolaevulinate dehydratase attached to Sepharose 4B is reported. 2. 2. When insolubilized enzyme was treated with 3 and 6 M urea, non covalently bound subunits were dissociated and detected in the el...

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Detalles Bibliográficos
Autores principales: Batlle, Alcira María del Carmen, Stella de Rosellini, Ana María Cristina, Ferramola, Ana María, Sancovich, Horacio Alberto
Publicado: 1978
Materias:
enzyme
porphobilinogen synthase
porphyrin
animal experiment
cattle
liver
Animals
Cattle
Chemistry
Enzymes, Immobilized
Hydrogen-Ion Concentration
Kinetics
Liver
Macromolecular Substances
Models, Chemical
Porphobilinogen Synthase
Protein Denaturation
Sepharose
Solubility
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v9_n6_p401_DelCBatlle
http://hdl.handle.net/20.500.12110/paper_0020711X_v9_n6_p401_DelCBatlle
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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