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. Author manuscript; available in PMC: 2021 Sep 30.
Published in final edited form as: Arch Biochem Biophys. 2020 Jul 24;691:108477. doi: 10.1016/j.abb.2020.108477

Fig. 2.

Fig. 2.

Inhibition of ALDH9A1 by DEAB is reversible. (A) Progress curves from a dilution assay. ALDH9A1 (5 μM) was incubated with 10 μM DEAB and 1 mM NAD+ at 4°C for 60 minutes, and then assayed for activity by diluting 10-fold into assay buffer containing 0.5 mM hexanal and 1 mM NAD+. (B) Residual activity after removing excess DEAB. ALDH9A1 (5 μM) was incubated with 10 μM DEAB and 1 mM NAD+ for 60 minutes, and then the excess DEAB was removed by spin ultrafiltration using Amicon Ultra-0.5 mL centrifugal filter units. The activity was then measured in an assay containing 0.5 mM hexanal and 1 mM NAD+. Prior to the enzyme assays, the enzyme concentration was measured and used to adjust the progress curves.