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Figure 3: SDS-PAGE (12 %) analysis of purification protocol fractions containing L-asparaginase II. (A): AspSP Purification protocol fractions of SDS-PAGE stained with Coomassie Blue: Lane 1: Protein molecular mass markers (Bench Mark™ Protein Ladder, Invitrogen); lane 2: soluble fraction after cell disruption; lane 3: sample after 1% (w/v) of streptomycin sulfate precipitation; lane 4: sample after dialysis and loaded on cation exchange Hiprep SP XL column; lane 5: pooled fractions of cation exchange chromatography loaded on Sephacryl S-200; and lane 6: homogeneous AspSP (34.5 kDa) after elution from size exclusion chromatography. (B): AspMP Purification protocol fractions of SDS-PAGE stained with Coomassie Blue: Lane 1: soluble fraction after cell disruption; lane 2: sample after 1% (w/v) of streptomycin sulfate precipitation; lane 3: sample after dialysis loaded on cation exchange Hiprep SP XL column; lane 4: homogeneous L-asparaginase II (34.5 kDa) pool eluted from the cation exchange column; and lane 5: Protein molecular mass markers (Low Range Protein Ladder, BIO-RAD). (C): SDS-PAGE stained with Silver of purified AspMP and AspSP proteins: Lane 1: Protein molecular mass markers (Low Range Protein Ladder, BIO-RAD); lane 2: AspMP; and lane 3: AspSP. |