| 000 | 01261 a2200325 4500 | ||
|---|---|---|---|
| 005 | 20250512204104.0 | ||
| 264 | 0 | _c19810625 | |
| 008 | 198106s 0 0 eng d | ||
| 022 | _a0014-2956 | ||
| 024 | 7 |
_a10.1111/j.1432-1033.1981.tb05140.x _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aYasuda, Y | |
| 245 | 0 | 0 |
_aEvidence for the presence of two kinetically distinct active forms of ribonuclease T2. The pH dependence of the steady-state kinetic parameter, kcat, for transphosphorylation of both a natural and a synthetic substrate. _h[electronic resource] |
| 260 |
_bEuropean journal of biochemistry _cFeb 1981 |
||
| 300 |
_a229-34 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aBuffers |
| 650 | 0 | 4 |
_aEndonucleases _xmetabolism |
| 650 | 0 | 4 | _aEndoribonucleases |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 |
_aIsoenzymes _xmetabolism |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 |
_aRibonucleases _xmetabolism |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 700 | 1 | _aInoue, Y | |
| 773 | 0 |
_tEuropean journal of biochemistry _gvol. 114 _gno. 2 _gp. 229-34 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1111/j.1432-1033.1981.tb05140.x _zAvailable from publisher's website |
| 999 |
_c6260427 _d6260427 |
||