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Table 2 Effect of inhibitors on ATPase activity of the purified ATPase.

From: Na+-stimulated ATPase of alkaliphilic halotolerant cyanobacterium Aphanothece halophytica translocates Na+ into proteoliposomes via Na+ uniport mechanism

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

  1. 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.