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. Author manuscript; available in PMC: 2015 Jul 1.

Published in final edited form as: J Biomol Screen. 2014 Dec 4;20(5):663–672. doi: 10.1177/1087057114561400

(A) CtBP1 enzymatic activity (nmol NADH/min/mg protein) was determined spectrophotometrically in the presence of 150 μM NADH and the indicated concentrations of NSC95397 ( ) and MTOB (■). No activity was observed in the absence of substrate. (B) NSC95397 is unable to inhibit another NADH dependent enzyme, LDH. NSC95397 did not significantly inhibit enzymatic activity in the presence of 5 μM pyruvate (■) nor did it exhibit significant consumption of NADH without pyruvate ( ). (C) The effect of a known substrate, MTOB, on the CtBP1-E1A interaction was monitored using both the AlphaScreen and fluorescence polarization assays. NSC95397 (▼) was able to disrupt the interaction, while MTOB (■), the more efficient CtBP1 substrate, was ineffective at disrupting the interaction.

Inline graphic — (A) CtBP1 enzymatic activity (nmol NADH/min/mg protein) was determined spectrophotometrically in the presence of 150 μM NADH and the indicated concentrations of NSC95397 ( ) and MTOB (■). No activity was observed in the absence of substrate. (B) NSC95397 is unable to inhibit another NADH dependent enzyme, LDH. NSC95397 did not significantly inhibit enzymatic activity in the presence of 5 μM pyruvate (■) nor did it exhibit significant consumption of NADH without pyruvate ( ). (C) The effect of a known substrate, MTOB, on the CtBP1-E1A interaction was monitored using both the AlphaScreen and fluorescence polarization assays. NSC95397 (▼) was able to disrupt the interaction, while MTOB (■), the more efficient CtBP1 substrate, was ineffective at disrupting the interaction.