Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8334275 | International Journal of Biological Macromolecules | 2012 | 5 Pages |
Abstract
Reactive oxygen species (ROS) can damage the lipids, proteins and DNA when produced excessively in cells. Here, we describe the isolation and identification of a novel antioxidant protein named SmP90 from the nematocyst of jellyfish Stomolophus meleagris by 50% ammonium sulfate precipitation and gel filtration chromatography, superdex75. HPLC and SDS-PAGE analysis revealed >95% purity of SmP90 with apparent molecular weight of 90 kDa, approximately. The identification of SmP90 was confirmed by both N-terminal amino acids sequencing, with the sequences of NLDTPYCFYSGDYGG, and peptide mass fingerprint (PMF) analysis by MALDI-TOF-MS. However, no known protein had been completely matched in the database, which indicated that SmP90 might be a novel protein. The antioxidant assay result showed that it had strong superoxide anion radical-scavenging activity with the half-scavenging concentration (EC50) of about 16 μg/mL. Therefore, the present study is the first time to demonstrate a high efficient method of isolating a novel antioxidant protein from the nematocyst of jellyfish S. meleagris.
Keywords
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Biochemistry
Authors
Rongfeng Li, Huahua Yu, Ronge Xing, Song Liu, Yukun Qing, Kecheng Li, Bing Li, Xiangtao Meng, Jinhui Cui, Pengcheng Li,