Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes.
Biochem Biophys Res Commun
; 221(1): 117-21, 1996 Apr 05.
Article
en En
| MEDLINE
| ID: mdl-8660320
ABSTRACT
A GSH-dependent dehydroascorbate reductase (EC 1.8.5.1) was purified to homogeneity from human erythrocytes. The enzyme was a monomer of 32 kDa and was purified 133-fold from a crude DEAE-Sepharose fraction with a 25% yield. The reduced protein had a pI of 5.1 as judged by isoelectric focusing. Kinetic analysis gave a Kcat of 316 min-1, a Km of 0.21 mM for DHA with a Kcat/Km of 2.47 x 10(4) M-1 sec-1, and a Km of 3.5 mM for GSH with a Kcat/Km of 1.51 x 10(3) M-1 sec-1. This is the second DHA reductase (after thioltransferase) isolated from human erythrocytes, but unlike thioltransferase, it has no thiol-disulfide oxido-reductase activity.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oxidorreductasas
/
Proteína Disulfuro Reductasa (Glutatión)
/
Eritrocitos
/
Glutatión
Límite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1996
Tipo del documento:
Article
País de afiliación:
Estados Unidos