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. Author manuscript; available in PMC: 2007 Aug 14.

Published in final edited form as: Toxicon. 2007 Jan 10;49(7):899–908. doi: 10.1016/j.toxicon.2006.12.013

Fig.7 — Effect of eristostatin mutants in C8161 cell wound closure on fibronectin and on platelet aggregation. The same batch of recombinant eristostatin or its mutants was used to do both sets of experiments. (A) The IC₅₀ values of R27, G28, D29 and N31 were infinity because those mutants showed no inhibitory effect on ADP-induced platelet aggregation. (B) Activities of mutants assayed by C8161 in vitro wound closure on fibronectin. The percent closure was calculated as previously described. The values represent the means (± SE, vertical bars) of nine independent experiments. wtEr =wild type eristostatin; each amino acid is represent by a single letter code. * indicates mutations with significant loss of inhibition in both assays.

Fig.7 — Effect of eristostatin mutants in C8161 cell wound closure on fibronectin and on platelet aggregation. The same batch of recombinant eristostatin or its mutants was used to do both sets of experiments. (A) The IC₅₀ values of R27, G28, D29 and N31 were infinity because those mutants showed no inhibitory effect on ADP-induced platelet aggregation. (B) Activities of mutants assayed by C8161 in vitro wound closure on fibronectin. The percent closure was calculated as previously described. The values represent the means (± SE, vertical bars) of nine independent experiments. wtEr =wild type eristostatin; each amino acid is represent by a single letter code. * indicates mutations with significant loss of inhibition in both assays.