Reductase domain cysteines 1048 and 1114 are critical for catalytic activity of human endothelial cell nitric oxide synthase as probed by site-directed mutagenesis

Biochemical and Biophysical Research Communications

Volumn 226, Issue 1, 1996, Pages 293-300

  Zhang, J L ^b   Patel, J M ^a,b   Li, Y D ^b   Block, E R ^b  

^a VETERANS AFFAIRS MEDICAL CENTER   (United States)

^b UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CITRULLINE; CYSTEINE; ISOENZYME; NITRIC OXIDE SYNTHASE; OLIGONUCLEOTIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

AMINO ACID METABOLISM; ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; ELECTRON TRANSPORT; ENDOTHELIUM CELL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GENETIC CONSERVATION; HUMAN; HUMAN CELL; IMMUNOBLOTTING; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ANIMALIA;

EID: 0030568829     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.1348     Document Type: Article

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