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. 2010 Feb 6;47(5):423–431. doi: 10.1159/000281582

Fig. 3.

Fig. 3

Activity of specific MMPs in the SHR plasma in gelatin zymography. The protease activity in plasma was confirmed by gel zymography using molecular weight standards for confirmation. Enhanced pro- and active-MMP-9 (92/86 kDa), MMP-2 (72/66 kDa), as well as MMP-7 (∼20 kDa) activities were detected in the SHR plasma (b). The bar graphs (a) represent measurements of active MMP levels. As control, we showed that all MMP activity is blocked in vitro by metal chelation (EDTA) and we confirmed by gel zymography with a serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), that the enhanced proteolytic activity in the SHR was not affected by serine protease inhibition (b).