. 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 4.

Hydrolysis of the Triphosphate Derivatives as Substrates of Rat NTPDase1 (Ectoapyrase) and NTPDase2 (Ecto-ATPase) Stably Expressed in CHO Cells

substrate	activity^a (%)
substrate	NTPDase1	NTPDase2
ATP	100	100
6a, (N)-methanocarba-ATP³⁹	52	4
6c, (S)-(±)-methanocarba-ATP³⁹	57	34

The hydrolysis rate with the two derivatives as substrate is compared to that of ATP (100%) for each enzyme. Values are means of two experiments with duplicate determinations in each. Nontransfected CHO cells were analyzed as control. They contained no significant activity for the extracellular hydrolysis of ATP. 100% values correspond to the following: NTPDase1, 42.1 nmol/(min 10⁶ cells); NTPDase2, 13.5 nmol/(min 10⁶ cells).