Fig. 2
From: Shrimp (Pandalopsis dispar) waste hydrolysate as a source of novel β–secretase inhibitors
Purification steps of β–secretase inhibitory peptide from SWH24 by Sephadex G–25 column chromatography and HPLC. I Sephadex G–25 Gel filtration chromatogram of hydrolysates prepared with SWH24 (b, lower layer). Separation was performed with 1.5 ml/min and collected at a fraction volume of 7.5 ml. The fractions isolated by Sephadex G–25 Gel column were separated (A ~ D) and β–secretase activity determined as upper panel (a). II,III,IV HPLC chromatogram of potent β–secretase inhibitory activity of separated fraction from previous step. Separation was performed with linear gradient of acetonitrile at a flow rate of 1.0 ml/min and Grom–sil 120 ODS–5 ST column (5 μm, 10 × 250 mm). Elution was monitored at 215 nm (b, lower layer). The fractions showing β–secretase inhibitory activity were determinded IC50 (mg/ml) as shown in upper layer (a)