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. Author manuscript; available in PMC: 2012 Oct 4.
Published in final edited form as: Biochemistry. 2011 Sep 12;50(39):8417–8426. doi: 10.1021/bi200802w

Figure 5.

Figure 5

PAFAH-II activity assays. Relative enzyme activity (mAbs/min) was determined using the substrate 2-thio-PAF. (A) Enzymatic activity of PAFAH-II constructs in whole HEK293 cell lysates is reported from three independent experiments. (B) Relative enzymatic activity of WT-PAFAH-II-YFP from unstressed and stressed HEK293 cells are shown from the insoluble fractions of three independent experiments. The asterisk indicates a statistically significant increase in activity between unstressed and stressed samples (student t-test, p=0.028). Activity of G2A-PAFAH-II-YFP and Triple-mutant-PAFAH-II-CFP was undetectable in the insoluble fraction (data not shown). (C) Enzymatic activity of unmyristoylated, GST-tagged WT and Triple-mutant-PAFAH-II expressed and purified from E. coli are compared to show the effect of the triple mutation on enzyme activity.