| 000 | 01329 a2200397 4500 | ||
|---|---|---|---|
| 005 | 20250512133131.0 | ||
| 264 | 0 | _c19700601 | |
| 008 | 197006s 0 0 eng d | ||
| 022 | _a0014-2956 | ||
| 024 | 7 |
_a10.1111/j.1432-1033.1970.tb00892.x _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aCreighton, T E | |
| 245 | 0 | 0 |
_aA steady-state kinetic investigation of the reaction mechanism of the tryptophan synthetase of Escherichia coli. _h[electronic resource] |
| 260 |
_bEuropean journal of biochemistry _cMar 1970 |
||
| 300 |
_a1-10 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aChromatography, Gel |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aFeedback |
| 650 | 0 | 4 | _aFluorescence |
| 650 | 0 | 4 | _aGlyceraldehyde |
| 650 | 0 | 4 | _aGlycerides |
| 650 | 0 | 4 |
_aHydro-Lyases _xantagonists & inhibitors |
| 650 | 0 | 4 | _aIndoles |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Biological |
| 650 | 0 | 4 | _aModels, Chemical |
| 650 | 0 | 4 | _aModels, Structural |
| 650 | 0 | 4 | _aPhosphoric Acids |
| 650 | 0 | 4 | _aPyridoxal Phosphate |
| 650 | 0 | 4 | _aSerine |
| 650 | 0 | 4 | _aTryptophan |
| 773 | 0 |
_tEuropean journal of biochemistry _gvol. 13 _gno. 1 _gp. 1-10 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1111/j.1432-1033.1970.tb00892.x _zAvailable from publisher's website |
| 999 |
_c4911960 _d4911960 |
||