| 000 | 01500 a2200493 4500 | ||
|---|---|---|---|
| 005 | 20250512144802.0 | ||
| 264 | 0 | _c19720511 | |
| 008 | 197205s 0 0 eng d | ||
| 022 | _a0006-2960 | ||
| 024 | 7 |
_a10.1021/bi00801a011 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aGabel, D | |
| 245 | 0 | 0 |
_aChanges in conformation of insolubilized trypsin and chymotrypsin, followed by fluorescence. _h[electronic resource] |
| 260 |
_bBiochemistry _cDec 1971 |
||
| 300 |
_a4661-9 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aAlanine |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCarboxylic Acids |
| 650 | 0 | 4 |
_aChymotrypsin _xantagonists & inhibitors |
| 650 | 0 | 4 | _aCyanogen Bromide |
| 650 | 0 | 4 | _aHot Temperature |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 | _aMathematics |
| 650 | 0 | 4 | _aNaphthalenes |
| 650 | 0 | 4 | _aPeptides |
| 650 | 0 | 4 | _aPolysaccharides |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aProtein Denaturation |
| 650 | 0 | 4 | _aSolubility |
| 650 | 0 | 4 |
_aSpectrometry, Fluorescence _xinstrumentation |
| 650 | 0 | 4 | _aSulfonic Acids |
| 650 | 0 | 4 | _aTemperature |
| 650 | 0 | 4 | _aToluidines |
| 650 | 0 | 4 | _aTrypsin |
| 650 | 0 | 4 | _aTrypsin Inhibitors |
| 650 | 0 | 4 | _aTryptophan |
| 650 | 0 | 4 | _aUrea |
| 700 | 1 | _aSteinberg, I Z | |
| 700 | 1 | _aKatchalski, E | |
| 773 | 0 |
_tBiochemistry _gvol. 10 _gno. 25 _gp. 4661-9 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1021/bi00801a011 _zAvailable from publisher's website |
| 999 |
_c5142428 _d5142428 |
||