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. 2008 Oct 15;3(10):e3414. doi: 10.1371/journal.pone.0003414

Figure 1. Purification and amino acid sequence of HWTX-XI.

Figure 1

(A) Ion-exchange HPLC chromatograph of crude Ornithoctonus huwena venom. The column (Waters Protein-Pak CM, 10 mm×100 mm) was equilibrated with 0.1 M sodium phosphate buffer, pH 6.8, the crude venom (10 mg in 2 ml) was loaded and eluted at a flow rate of 3 mL/min, using a gradient of 0–81% buffer B (1 M NaCl, 0.1 M sodium phosphate buffer, pH 6.8 ) over 60 min. Then the peak E was applied to Vydac C18 reverse phase column (4.6 mm×250 mm) equilibrated with 0.1% trifluoroacetic acid (B), using a gradient of 20–40% buffer C (0.1% trifluoroacetic acid in acetonitrile) over 45 min. The fraction of retention time 12.30 min containing HWTX-XI was further purified by Vydac C18 rpHPLC as shown in the left inset. The molecular mass of HWTX-XI was determined by MALDI-TOF mass spectrometry (right inset of B). (C) Amino acid sequence of HWTX-XI determined by Edman degradation. (D) The oligonucleotide sequence of HWTX-XI cDNA. The cDNA encoding the mature peptide are underlined. The polyadenylations signal, AATAAA, is double underlined.