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Figure 2 | BMC Biochemistry

Figure 2

From: Purification and characterization of cysteine protease from germinating cotyledons of horse gram

Figure 2

SDS-PAGE analysis of the fractions from each step of endoprotease (EP-HG) purification from the cotyledons of germinating horse gram seeds and seedlings. Conc. of protein loaded on each well in gel is 100 ug. Lane 1. Crude extract, Lane 2. Protein from 30-60% saturated ammonium sulfate fraction. Lane 3. Pooled fractions (14-20) after DEAE-Cellulose chromatography. Lane 4. Unbound fraction from CM-Sephacel column. Lane 5. Molecular weight markers consisting of Phosphorylase b (94 k Da), BSA (67 k Da), ovalbumin (43 k Da), carbonic anhydrase (30 k Da), soybean trypsin inhibitor (20.1 k Da) and α-lactalbumin (14.4 k Da).

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