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. 2010 Mar 12;5(3):e9687. doi: 10.1371/journal.pone.0009687

Figure 1. Rotofor based separation of B. g. rhinoceros venom proteins.

Figure 1

A. SDS-PAGE (10%) was run with 50 µg of B. g. rhinoceros venom and stained with Coomassie brilliant blue. Several proteins with different molecular weights are present in this venom. B. 2 mg of venom were mixed with non-reducing rotofor buffer containing ampholytes with pI 6–8 and separated under non-denaturing conditions. In total 10 fractions (indicated by the numbers at the top of the gel) were collected. 10 µl of each fraction were run in SDS-PAGE (10%) and stained with Coomassie brilliant blue. C. 20 µl of each rotofor fraction were used to measure serine protease activity using Arg-AMC fluorescent substrate. The data represents the mean ± S.D. (n = 3). The hydrolytic activity measured for fraction 5 was taken as 100%.