Recombinant Nox4 cytosolic domain produced by a cell or cell-free base systems exhibits constitutive diaphorase activity

Biochemical and Biophysical Research Communications

Volumn 419, Issue 3, 2012, Pages 453-458

  Nguyen, Minh Vu Chuong ^a   Zhang, Leilei ^a   Lhomme, Stanislas ^b   Mouz, Nicolas ^b   Lenormand, Jean Luc ^c   Lardy, Bernard ^a   Morel, Françoise ^a  

^a CNRS   (France)

^b MINATEC   (France)

^c LABORATOIRE TIMC IMAG   (France)

Author keywords

Cell free protein expression; Diaphorase activity; NADPH oxidase Nox4; Truncated recombinant proteins

Indexed keywords

CYTOCHROME C; DIHYDROLIPOAMIDE DEHYDROGENASE; IODONITRO TETRAZOLIUM CHLORIDE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; TETRAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL FREE SYSTEM; CYTOSOL; ELECTRON TRANSPORT; ENZYME ACTIVITY; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN METABOLISM; PROTEIN SYNTHESIS; TRANSLATION INITIATION;

CELL-FREE SYSTEM; CYTOSOL; ESCHERICHIA COLI; HEK293 CELLS; HUMANS; NADH DEHYDROGENASE; NADPH OXIDASE; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 84862790990     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.01.136     Document Type: Article

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