Gachhui, R <br/><br/>
Characterization of the reductase domain of rat neuronal nitric oxide synthase generated in the methylotrophic yeast Pichia pastoris. Calmodulin response is complete within the reductase domain itself.  [electronic resource] 

 -  The Journal of biological chemistry  Aug 1996 
 - 20594-602 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.271.34.20594  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Base Sequence<br/>Calmodulin--metabolism<br/>Calmodulin-Binding Proteins--metabolism<br/>DNA Primers--chemistry<br/>Electron Spin Resonance Spectroscopy<br/>Flavins--chemistry<br/>Flavoproteins--chemistry<br/>Isoenzymes--chemistry<br/>Molecular Sequence Data<br/>NADH Dehydrogenase--chemistry<br/>Neurons--enzymology<br/>Nitric Oxide Synthase--chemistry<br/>Oxidation-Reduction<br/>Pichia--genetics<br/>Rats<br/>Recombinant Proteins<br/>Spectrometry, Fluorescence<br/>Tryptophan--chemistry