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Fig. 3 | Fisheries and Aquatic Sciences

Fig. 3

From: Purification and characterization of β-secretase inhibitory peptide from sea hare (Aplysia kurodai) by enzymatic hydrolysis

Fig. 3

Identification of molecular weight and amino acid sequence of the purified peptide from sea hare muscle hydrolysate. MS/MS experiments were performed on a Q-TOF tandem mass spectrometer equipped with a nano-ESI source. All MS/MS spectra were acquired using a Thermo Finnigan (San Jose, CA, USA) LTQ mass spectrometer. Each full MS (m/z range, 100–2000) scan was followed by three MS/MS scans of the most abundant precursor ions in the MS spectrum with dynamic exclusion enabled. Sequencing of the purified peptides was acquired over the m/z range 100–1800 and sequenced by using de novo sequencing program

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