Figure 2: Double internal cleavages appear to inactivate neutrophil elastase. | Nature Communications

Figure 2: Double internal cleavages appear to inactivate neutrophil elastase.

From: Autoprocessing of neutrophil elastase near its active site reduces the efficiency of natural and synthetic elastase inhibitors

Figure 2

Neutrophil elastase was incubated with biotinylated AAPV-chloromethylketone (neutrophil elastase inhibitor) at 37 °C for 30 min. (a) Eight μg of wild-type or mutated mouse neutrophil elastase (wt mNE or mut mNE) was separated by SDS–PAGE and stained with Coomassie blue. There were equal amounts of band 3 and 4. (b) One μg of each mouse neutrophil elastase form was separated by SDS–PAGE and analysed by western blotting using avidin-HRP. The signal for band 3 was much stronger compared with band 4. (c) Scheme showing the molecular structure of the three neutrophil elastase bands. The lowest band (4) contains single-nicked mouse neutrophil elastase as well as double-nicked mouse neutrophil elastase. The double-nicked mouse neutrophil elastase does not appear to react with the chloromethylketone as judged from the reduced western blot signal (b) in comparison with the total amount of the tc neutrophil elastase (a). The experiment was repeated thrice.

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