Table 3.
Hydrolysis Rates of Monophosphate Derivatives as Substrates of Purified Recombinant Rat Ecto-5′-nucleotidase
| substrate | activitya (%) |
|---|---|
| AMP | 100 |
| 7a, (N)-methanocarba-AMP39 | 0.14 |
| 7c, (S)-(±)-methanocarba-AMP39 | 0.0 |
Values are means of two experiments with duplicate determinations in each. The catalytic activity in the presence of AMP (100%) corresponded to 5.6 nmol/(min μg) protein.