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KMID : 0043320110340060893
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Archives of Pharmacal Research
2011 Volume.34 No. 6 p.893 ~ p.899
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Bioassay-guided isolation of a novel protein with antitumor activity from Trachyrhamphus serratus (Syngnathidae)
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Wang Meng Yue
Qin Sun Xing
He Fen
Li Xiaobo
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Abstract
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A novel protein with antitumor activity, Hailongin, was purified from the aqueous extract of the whole body of Trachyrhamphus serratus, which is commonly used in traditional Chinese medicine, by bioassay-guided fractionation. Hailongin exhibited strong inhibition of proliferation of the tested human cell lines, such as A549, HeLa, LoVo and CCRF-CEM. The IC50 values of Hailongin ranged from 5.4 to 25.7 μ/mL. An in vivo study showed that the growth of implanted S-180 solid tumors in mice was significantly inhibited by Hailongin treatment, while the immunological function of the tumor-bearing mice was enhanced. The molecular weight and the isoelectric point of Hailongin were 57.074 kDa (by MALDI-TOF-MS) and 6.2 (by isoelectric focusing-polyacrylamide gel electrophoresis), respectively. Seventeen amino acids were identified in Hailongin. The acidic amino acids accounted for the majority of Hailongin’s amino acid composition. The N-terminal amino acid sequence of Hailongin was determined to be IVPYSHNAGNKGLTQMR and showed no significant homology with known proteins.
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KEYWORD
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Antitumor, Isolation, Protein, Trachyrhamphus serratus
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