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Fig. 2 | Fisheries and Aquatic Sciences

Fig. 2

From: Characterization of antioxidative peptide purified from black eelpout (Lycodes diapterus) hydrolysate

Fig. 2

Steps for the purification of DPPH radical scavenging activity peptide from black eelpout muscle hydrolysate. I Sephadex G-25 Gel filtration chromatogram of hydrolysates. Gel filtration chromatogram of hydrolysates prepared with black eelpout muscle. 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 DPPH radical scavenging activity was determined as upper panel. II, III Reverse phase-HPLC chromatograms of the potent DPPH radical scavenging activity fractions from the previous steps. The lower panels of each pair show the chromatography results of separated fractions while the top panels of each pair represent the DPPH radical scavenging activity of separated fractions in terms of their EC50 values expressed in mg/mL (I) or μg/mL (II, III). Statistical significance was determined by ANOVA

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