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Bioassay-guided isolation of a novel protein with antitumor activity from Trachyrhamphus serratus (Syngnathidae).
MedLine Citation:
PMID:  21725809     Owner:  NLM     Status:  In-Data-Review    
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 IC(50) 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.
Meng Yue Wang; Sun Xing Qin; Fen He; Xiaobo Li
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Publication Detail:
Type:  Journal Article     Date:  2011-07-02
Journal Detail:
Title:  Archives of pharmacal research     Volume:  34     ISSN:  0253-6269     ISO Abbreviation:  Arch. Pharm. Res.     Publication Date:  2011 Jun 
Date Detail:
Created Date:  2011-07-04     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8000036     Medline TA:  Arch Pharm Res     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  893-9     Citation Subset:  IM    
School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
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