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Titel:

Thermodynamic analysis of L-arginine and N omega-hydroxy-L-arginine binding to nitric oxide synthase.

Dokumenttyp:
Journal Article; Research Support, Non-U.S. Gov't
Autor(en):
Zakariassen, H; Cederkvist, FH; Harbitz, E; Shimizu, T; Lange, R; Mayer, B; Gorren, AC; Andersson, KK; Sørlie, M
Abstract:
Isothermal titration calorimetry has been used to determine thermodynamic parameters of substrate binding to the oxygenase domain of neuronal nitric oxide synthase (nNOS(oxy)) in the presence of the cofactor tetrahydrobiopterin. The intermediate N(omega)-hydroxy-L-arginine (NHA) has a larger affinity than L-Arginine (L-Arg) for nNOS(oxy), with K(d)=0.4+/-0.1 microM and 1.7+/-0.3 microM at 25 degrees C, respectively. nNOS(oxy) binds NHA and L-Arg with DeltaH -4.1+/-0.2 and -1.0+/-0.1 kcal/mol and...     »
Zeitschriftentitel:
Biochim Biophys Acta
Jahr:
2008
Band / Volume:
1784
Heft / Issue:
5
Seitenangaben Beitrag:
806-10
Sprache:
eng
Volltext / DOI:
doi:10.1016/j.bbapap.2008.02.016
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/18371313
Print-ISSN:
0006-3002
TUM Einrichtung:
Klinik für Herz- und Gefäßchirurgie (Prof. Lange)
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