Table 2 |
|
|
Effect of inhibitors on ATPase activity of the purified ATPase. |
|
|
Addition |
Residual ATPase activity (%) |
|
|
|
|
None |
100 |
|
1 mM CCCP |
107 |
|
0.5 mM NEM |
102 |
|
50 mM KNO3 |
103 |
|
20 mM KSCN |
101 |
|
1 mM Ouabain |
115 |
|
0.01 mM Orthovanadate |
100 |
|
0.2 mM Amiloride |
98 |
|
5 mM Sodium azide |
64 |
|
1 mM DCCD |
78 |
|
|
|
|
ATP hydrolytic activity was assayed in the reaction mixture containing 20 mM Tris-HCl pH 7.6, 5 mM MgCl2, 10 mM NaCl and the purified ATPase (30 μg protein). The reaction was started by the addition of 4 mM ATP (Tris salt). Each inhibitor was added to the reaction mixture 10 min before the start of the reaction. One hundred percent activity corresponded to 450 nmol min-1 (mg protein)-1. |
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|
Soontharapirakkul and Incharoensakdi BMC Biochemistry 2010 11:30 doi:10.1186/1471-2091-11-30 |
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