Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis

The detection and accumulation of tetrapyrrole intermediates synthesized by the action of bovine liver porphobilinogen deaminase immobilized to Sepharose 4B is reported. Employing Sepharose‐deaminase preparations, two phases in uroporphyrinogen I synthesis as a function of time were observed, sugges...

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Detalles Bibliográficos
Autores principales: Kotler, M.L., Juknat, A.A., Fumagalli, S.A., Batlle, A.M.
Formato: JOUR
Materias:
immobilized enzyme
porphobilinogen deaminase
uroporphyrinogen
animal
article
biosynthesis
biotechnology
cattle
enzyme specificity
enzymology
in vitro study
kinetics
liver
metabolism
Animal
Biotechnology
Cattle
Enzymes, Immobilized
Hydroxymethylbilane Synthase
In Vitro
Kinetics
Liver
Substrate Specificity
Support, Non-U.S. Gov't
Uroporphyrinogens
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_08854513_v13_n2_p173_Kotler
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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