Inactivation of NADPH oxidase from human neutrophils by affinity labeling with pyridoxal 5'-diphospho-5'-adenosine.
Biochem Biophys Res Commun
; 181(3): 1259-65, 1991 Dec 31.
Article
em En
| MEDLINE
| ID: mdl-1764075
ABSTRACT
When a particulate NADPH oxidase prepared from phorbol ester-activated human neutrophils was treated with pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP), the superoxide anion-producing activity was inhibited according to affinity labeling kinetics. NADPH afforded a protection against inactivation which was competitive with respect to PLP-AMP; 2',5'-ADP and 2'-phospho-5' diphosphoadenosine (ATP ribose) appeared to be as potent as NADPH as protecting agents. NADP+ and ATP were less effective, while ADP and GTP-gamma-S did not protect significantly. These results suggest that PLP-AMP can be used, in conjunction with tritiated cyanoborohydride, to identify the elusive NADPH-dependent flavoprotein which is part of the electron transfer chain of NADPH oxidase.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfato de Piridoxal
/
Marcadores de Afinidade
/
Difosfato de Adenosina
/
NADH NADPH Oxirredutases
/
NADP
/
Neutrófilos
Limite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
França