Purification and Characterization of a Novel Intracellular Sucrase Enzyme of Leishmania donovani Promastigotes

Figure 2

Gel electrophoretic analysis and activity staining of purified intracellular sucrase. (a) Electrophoresis (10% SDS-PAGE) was done in a discontinuous buffer system. Lane 1: molecular mass standards indicated on the left are as follows: galactosidase (116 kDa), phosphorylase B (97.4 kDa), bovine serum albumin (66 kDa), ovalbumin (45 kDa), carbonic anhydrase (29 kDa); lane 2 shows the purified intracellular sucrase protein band of nearly ~56 kDa in size. (b) 10% SDS-PAGE standard curve plotted with logarithm of the molecular weight against relative mobility. The arrow indicates the log of molecular weight of intracellular sucrase subunit in 10% SDS-PAGE. (c) Substrate staining of purified intracellular sucrase in native gel; the arrow indicates the activity band in native gel. (d) Coomassie stained purified intracellular sucrase in native gel. Lane 1 represents the proteins galactosidase (116 kDa) and phosphorylase B (97.4 kDa) as molecular weight marker and lane 2 shows the native form of purified intracellular sucrase.