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. Author manuscript; available in PMC: 2009 May 10.
Published in final edited form as: Mol Carcinog. 2008 May;47(5):326–337. doi: 10.1002/mc.20389

Figure 2.

Figure 2

Figure 2

Figure 2

The isolated RhoGAP domain shows greatly enhanced catalytic activity for RhoA, RhoB, RhoC and Cdc42. Recombinant full length and an isolated RhoGAP catalytic domain fragment (amino acids 609-878) of DLC-1 were expressed and purified for analysis of in vitro GAP activity. Real time GTP hydrolysis was measured with a fluorescently labeled PBP, as described in Fig. 1, for GST fusion proteins of wild type (A, B) RhoA, (C, D) RhoB, (E, F) RhoC, (G, H) Cdc42, and (I, J) Rac1. Data shown are representative of three independent experiments.