KCl-Dependent Release of Mitochondrial Membrane-Bound Arginase Appears to Be a Novel Variant of Arginase-II

Figure 4

Showing impact of concentration of KCl in homogenizing medium on the activity of arginase. E1 shows the experimental set 1 described in the text. (a) The activity of arginase in cytosolic fraction. Data is mean of three experiments and histogram represents mean ± SD; . (b) The anti-arginase-I cross reacts with the single band of 40 kDa in cytosolic fraction and their activity increases with increasing KCl concentration in homogenizing medium. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is taken as loading control. This result indicates the solubilisation of arginase-I proteins from the membrane of mitochondrial as well as other subcellular organelles. (c) The arginase activity decreases in the mitochondrial fraction with the increasing KCl concentration. But the percent decrease in the activity of the mitochondrial arginase-II is less than increase in the activity of cytosolic arginase-I; . (d) Anti-arginase-II has cross reactivity with the single band of the 40 kDa of mitochondrial fraction. The intensity of this band was decreased with increasing KCl concentration. Cytochrome C (Cyt C) was taken as loading control.

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