Abstract
Hepatocyte growth factor activator inhibitor type 2 (HAI-2) was identified as a potent inhibitor of hepatocyte growth factor activator (HGF activator). The primary translation product of HAI-2 contains two Kunitz domains. To characterize their function, we introduced a point mutation into the reactive site of each Kunitz domain, and assayed the mutants for their HGF activator inhibitory activity. A point mutation in the COOH-terminal Kunitz domain did not affect the activity of HAI-2, whereas a point mutation in the NH 2-terminal Kunitz domain markedly reduced the activity. These results suggest that the NH 2-terminal Kunitz domain is mainly responsible for the HGF activator inhibitory activity of HAI-2.
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