Author(s): Tanuma S, Tsai YJ, Sakagami H, Konno K, Endo H
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Abstract (ADP-ribose)n glycohydrolase activity was inhibited in vitro by lignin, a naturally occurring polymethoxyphenolic compound. However, coniferyl alcohol, which is a main component of lignin, was not inhibitory even at 100 micrograms/ml. Lignin caused competitive inhibition with respect to the substrate (ADP-ribose)n and its Ki value was 18 micrograms/ml. These results suggest that lignin with a polymerized structure has a functional domain that interacts with the (ADP-ribose)n glycohydrolase molecule at the same site as (ADP-ribose)n.
This article was published in Biochem Int
and referenced in Pharmaceutica Analytica Acta