Skip to main content
. Author manuscript; available in PMC: 2016 Jul 25.
Published in final edited form as: J Med Chem. 2002 May 9;45(10):2090–2100. doi: 10.1021/jm010538v

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
a

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.