Domains of macrophage NO synthase have divergent roles in forming and stabilizing the active dimeric enzyme

Biochemistry

Volumn 35, Issue 5, 1996, Pages 1444-1449

  Ghosh, Dipak K ^a   Abu Soud, Husam M ^a   Stuehr, Dennis J ^a,b  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BIOPTERIN; CYTOCHROME C; DITHIOTHREITOL; HEME; MONOMER; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; OXYGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UREA; PEPTIDE FRAGMENT;

ARTICLE; CATALYSIS; DIMERIZATION; DISSOCIATION; ENZYME STABILITY; PRIORITY JOURNAL; PROTEIN FOLDING; REDUCTION; BIOLOGICAL MODEL; BIOSYNTHESIS; CHEMISTRY; COMPARATIVE STUDY; DRUG EFFECT; ENZYMOLOGY; MACROPHAGE; PROTEIN CONFORMATION; PROTEIN DENATURATION;

ENZYME STABILITY; MACROPHAGES; MODELS, BIOLOGICAL; NITRIC OXIDE SYNTHASE; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; UREA;

EID: 0029664605     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9521295     Document Type: Article

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