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. 2016 Sep 9;6:33149. doi: 10.1038/srep33149

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Copyright © 2016, The Author(s)

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(A) A schematic diagram of HGF protein. A disulfied-bond between Cys487 and Cys604²⁷ and the 5 amino-acid sequences in the protease-cleavage sites of wild-type and engineered HGF proteins are indicated. A free cystein residue, Cys561, was mutated to serine (C561S) in some of the recombinant proteins used in this study. (B) Cellular Met activation by HGF, tcHGF(Xa), and scHGF(Xa). EHMES-1 cells were stimulated with indicated concentrations of recombinant HGF protein for 10 min. The cells were fixed and Met activation was detected by anti-phospho-Met (Tyr1234/1235) antibody. The activities were expressed as a relative Met phosphorylation calculated as described in the Method. Data are mean ± SD of six (HGF and tcHGF(Xa)) or four (scHGF(Xa)) independent experiments.