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