000 | 01856 a2200529 4500 | ||
---|---|---|---|
005 | 20250511180514.0 | ||
264 | 0 | _c19921216 | |
008 | 199212s 0 0 eng d | ||
022 | _a0021-9258 | ||
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aCantor, A B | |
245 | 0 | 0 |
_aLysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides. _h[electronic resource] |
260 |
_bThe Journal of biological chemistry _cNov 1992 |
||
300 |
_a23349-56 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 | _aAnimals |
650 | 0 | 4 | _aBase Sequence |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aCarbohydrate Conformation |
650 | 0 | 4 | _aCarbohydrate Sequence |
650 | 0 | 4 |
_aCathepsin D _xgenetics |
650 | 0 | 4 | _aChromatography, Affinity |
650 | 0 | 4 | _aChromatography, Ion Exchange |
650 | 0 | 4 | _aCloning, Molecular |
650 | 0 | 4 |
_aEnzyme Precursors _xgenetics |
650 | 0 | 4 | _aFemale |
650 | 0 | 4 |
_aGlycopeptides _xbiosynthesis |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 |
_aKidney _xenzymology |
650 | 0 | 4 |
_aLysosomes _xenzymology |
650 | 0 | 4 |
_aMannose _xmetabolism |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aOligodeoxyribonucleotides |
650 | 0 | 4 |
_aOligosaccharides _xmetabolism |
650 | 0 | 4 |
_aPepsinogens _xgenetics |
650 | 0 | 4 | _aPhosphorylation |
650 | 0 | 4 |
_aPhosphotransferases _xmetabolism |
650 | 0 | 4 | _aPlasmids |
650 | 0 | 4 | _aPolymerase Chain Reaction |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aTransferases (Other Substituted Phosphate Groups) |
650 | 0 | 4 | _aXenopus laevis |
700 | 1 | _aBaranski, T J | |
700 | 1 | _aKornfeld, S | |
773 | 0 |
_tThe Journal of biological chemistry _gvol. 267 _gno. 32 _gp. 23349-56 |
|
999 |
_c1337605 _d1337605 |