| 000 | 01864 a2200505 4500 | ||
|---|---|---|---|
| 005 | 20250513093118.0 | ||
| 264 | 0 | _c19961011 | |
| 008 | 199610s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 024 | 7 |
_a10.1074/jbc.271.34.20594 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aGachhui, R | |
| 245 | 0 | 0 |
_aCharacterization 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. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cAug 1996 |
||
| 300 |
_a20594-602 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. | ||
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aBase Sequence |
| 650 | 0 | 4 |
_aCalmodulin _xmetabolism |
| 650 | 0 | 4 |
_aCalmodulin-Binding Proteins _xmetabolism |
| 650 | 0 | 4 |
_aDNA Primers _xchemistry |
| 650 | 0 | 4 | _aElectron Spin Resonance Spectroscopy |
| 650 | 0 | 4 |
_aFlavins _xchemistry |
| 650 | 0 | 4 |
_aFlavoproteins _xchemistry |
| 650 | 0 | 4 |
_aIsoenzymes _xchemistry |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aNADH Dehydrogenase _xchemistry |
| 650 | 0 | 4 |
_aNeurons _xenzymology |
| 650 | 0 | 4 |
_aNitric Oxide Synthase _xchemistry |
| 650 | 0 | 4 | _aOxidation-Reduction |
| 650 | 0 | 4 |
_aPichia _xgenetics |
| 650 | 0 | 4 | _aRats |
| 650 | 0 | 4 | _aRecombinant Proteins |
| 650 | 0 | 4 | _aSpectrometry, Fluorescence |
| 650 | 0 | 4 |
_aTryptophan _xchemistry |
| 700 | 1 | _aPresta, A | |
| 700 | 1 | _aBentley, D F | |
| 700 | 1 | _aAbu-Soud, H M | |
| 700 | 1 | _aMcArthur, R | |
| 700 | 1 | _aBrudvig, G | |
| 700 | 1 | _aGhosh, D K | |
| 700 | 1 | _aStuehr, D J | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 271 _gno. 34 _gp. 20594-602 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.271.34.20594 _zAvailable from publisher's website |
| 999 |
_c8700076 _d8700076 |
||