| 000 | 01348 a2200397 4500 | ||
|---|---|---|---|
| 005 | 20250511125756.0 | ||
| 264 | 0 | _c19771028 | |
| 008 | 197710s 0 0 eng d | ||
| 022 | _a0006-3495 | ||
| 024 | 7 |
_a10.1016/S0006-3495(77)85611-7 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aDembo, M | |
| 245 | 0 | 0 |
_aA kinetic model of cooperativity in aspartate transcarbamylase. _h[electronic resource] |
| 260 |
_bBiophysical journal _cJun 1977 |
||
| 300 |
_a245-67 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 |
_aAdenosine Triphosphate _xmetabolism |
| 650 | 0 | 4 | _aAllosteric Regulation |
| 650 | 0 | 4 | _aAllosteric Site |
| 650 | 0 | 4 |
_aAspartate Carbamoyltransferase _xmetabolism |
| 650 | 0 | 4 |
_aAspartic Acid _xmetabolism |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 |
_aCarbamyl Phosphate _xmetabolism |
| 650 | 0 | 4 | _aCytosine Nucleotides |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aLigands |
| 650 | 0 | 4 | _aModels, Biological |
| 650 | 0 | 4 |
_aPhosphates _xmetabolism |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 650 | 0 | 4 |
_aSuccinates _xmetabolism |
| 700 | 1 | _aRubinow, S I | |
| 773 | 0 |
_tBiophysical journal _gvol. 18 _gno. 3 _gp. 245-67 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1016/S0006-3495(77)85611-7 _zAvailable from publisher's website |
| 999 |
_c354609 _d354609 |
||