Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: tetrahydrobiopterin binding kinetics and role of haem in dimerization.

The fatty-acylation-deficient bovine endothelial NO synthase (eNOS) mutant (Gly-2 to Ala-2, G2AeNOS) was purified from a baculovirus overexpression system. The purified protein was soluble and highly active (0.2-0.7 micromol of l-citrulline. mg-1.min-1), contained 0. 77+/-0.01 equivalent of haem per...

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Detalhes bibliográficos
Main Authors: List, B M, Klösch, B, Völker, C, Gorren, A C, Sessa, W C, Werner, E R, Kukovetz, W R, Schmidt, K, Mayer, B
Formato: Artigo
Idioma:Inglês
Publicado em: 1997
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1218289/
https://ncbi.nlm.nih.gov/pubmed/9173876
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