EC Number   |
Subunits |
Reference |
|---|
   3.4.21.6 | ? |
x * 45000, SDS-PAGE |
653968 |
| 3.4.21.6 | ? |
x * 59000, SDS-PAGE |
754844 |
| 3.4.21.6 | ? |
x * 60000, SDS-PAGE |
754909 |
| 3.4.21.6 | ? |
x * 65000, recombinant wild-type enzyme, SDS-PAGE |
652682 |
| 3.4.21.6 | dimer |
1 * 20000 + 1 * 30000, two bands detected, SDS-PAGE |
81419 |
| 3.4.21.6 | dimer |
and monomer. Dimer is about 1000000fold less active toward prothrombin than the monomer. Dimerization results in substantial change in tertiary or quarternary strucutre with a concomitant decrease in alpha-helix |
696780 |
| 3.4.21.6 | homodimer |
- |
752707 |
| 3.4.21.6 | monomer |
1 * 45000, SDS-PAGE |
650585 |
| 3.4.21.6 | monomer |
and dimer. Dimer is about 1000000fold less active toward prothrombin than the monomer. Dimerization results in substantial change in tertiary or quarternary strucutre with a concomitant decrease in alpha-helix |
696780 |
| 3.4.21.6 | More |
Ca2+, factor Xa and factor Va are part of the prothrombinase enzyme complex |
650336 |
