Figure 5 of Gupta, Mol Vis 2010; 16:2242-2252.

Figure 5. Inhibition of autodegrdation of βA3-crystalllin by protease inhibitors in the presence of CHAPS. The criterion for inhibition in the study was whether an inhibitor was able to prevent signature autodegradation of βA3-crystallin (50 μg, used with each inhibitor) into the three truncated specific I, II, and III. The inhibitors used in the study are identified at the top of the gel. Only the inhibitors of serine-type proteases such as phenylmethyl sulfonyl fluoride (PMSF, 2 mM, lane 2), aprotinin (25 μg/ml, lane 4) and chymostatin (lane 11) inhibited autodegradation of the crystallin, whereas 4(2-aminoehtyl)-benzene sulfonyl fluoride (2 mM, lane 3) showed partial inhibition of autodegradation. In contrast, the cysteine-protease inhibitors (E-64, 100 μM [lane 5], N-ethylmaleimide, 5 mM [lane 6] and iodoacetamide, 5 mM [lane 7], and metallo-proteinase inhibitors (EDTA, 5 mM [EDTA, lane 8] and ethylene glycotetraacetic acid, 5 mM [EGTA, lane 9] did not stop autodegradation of the crystallin.