| 000 | 01423 a2200409 4500 | ||
|---|---|---|---|
| 005 | 20250513073314.0 | ||
| 264 | 0 | _c19930901 | |
| 008 | 199309s 0 0 eng d | ||
| 022 | _a0264-6021 | ||
| 024 | 7 |
_a10.1042/bj2930357 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aXia, C | |
| 245 | 0 | 0 |
_aChemical modification of GSH transferase P1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site. _h[electronic resource] |
| 260 |
_bThe Biochemical journal _cJul 1993 |
||
| 300 |
_a357-62 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 |
_aArginine _xanalysis |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 |
_aCarboxylic Acids _xanalysis |
| 650 | 0 | 4 |
_aGlutathione _xmetabolism |
| 650 | 0 | 4 |
_aGlutathione Transferase _xantagonists & inhibitors |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 |
_aLysine _xanalysis |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aPeptide Fragments _xchemistry |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 700 | 1 | _aMeyer, D J | |
| 700 | 1 | _aChen, H | |
| 700 | 1 | _aReinemer, P | |
| 700 | 1 | _aHuber, R | |
| 700 | 1 | _aKetterer, B | |
| 773 | 0 |
_tThe Biochemical journal _gvol. 293 ( Pt 2) _gp. 357-62 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1042/bj2930357 _zAvailable from publisher's website |
| 999 |
_c8342392 _d8342392 |
||