Figure 9 of Srivastava, Mol Vis 2008; 14:1872-1885.

Figure 9. Comparison of properties of Arg-bond hydrolyzing proteinase isolated from the WS protein fraction, the α-crystallin fraction, the βH-crystallin fraction, and the membrane fraction of human lenses. A: Size-exclusion HPLC analysis is shown of the Arg-bond hydrolyzing proteinase purified from the WS protein fraction (red dotted line), the α-crystallin fraction (green dotted line), the βH-crystallin fraction (blue dotted line), and the membrane fraction (black dotted line). B: Nondenaturing gel electrophoresis is shown of the combined proteinase preparations from the WS protein fraction, α-crystallin fraction, βH-crystallin fraction, and membrane fraction. Note that a single proteinase peak was observed on combining proteinases isolated from all four fractions. C: Caseinolytic activity of the four proteinases isolated from WS-protein fraction (lane 1), α-crystallin fraction (lane 2), βH-crystallin fraction (lane 3), and membrane fraction (lane 4). Note that a co-migration caseinolytic activity of the four proteinases on a non-denaturation gel was observed.