EC Number   |
Subunits |
Reference |
|---|
    3.5.4.6 | ? |
x * 37000, SDS-PAGE |
667030 |
| 3.5.4.6 | ? |
x * 70000-95000, histidine-proline-rich-glycoprotein HPRG component, partially proteolyzed or deglycosylated, SDS-PAGE |
654859 |
| 3.5.4.6 | ? |
x * 78600, SDS-PAGE |
-, 755821 |
| 3.5.4.6 | ? |
x * 85390, SDS-PAGE |
-, 756756 |
| 3.5.4.6 | dimer |
- |
669453 |
| 3.5.4.6 | More |
enzyme contains a histidine-proline-rich-glycoprotein HPRG component, bound via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability, disulfide bridges are involved in formation of enzyme conformation |
654859 |
| 3.5.4.6 | More |
in contrast to AMP-deaminase isolated from the normal, healthy liver, where presence of relatively large (68 kDa) protein fragment is also detected, only smaller protein fragments are identified, while SDS-PAGE of AMP-deaminase isolated from the cirrhotic liver is performed |
670232 |
| 3.5.4.6 | More |
in enzyme from healthy liver beside immunologically reactive 92000 Da protein fragment, corresponding to the full size of the enzyme subunit, also a smaller, immunologically reactive protein fragment 68000 Da is identified in the gel. When SDS-PAGE of AMP-deaminase isolated from neo-plasmatic liver is performed only presence of protein fragment 68000 Da was detected |
670433 |
| 3.5.4.6 | More |
presence of two species of 173 kDa and 309 kDa being consistent with the existence of a dimer-tetramer equilibrium |
685351 |
| 3.5.4.6 | oligomer |
x * 68000, at least 3 different oligomeric forms of the enzyme, probably dimers, tetramers, and hexamers, SDS-PAGE |
656779 |
