Protein profiling analysis of skeletal muscle of a pufferfish, Takifugu rubripes
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Protein profile of the skeletal muscle of Takifugu rubripes, a kind of pufferfish, was carried out with two-dimensional polyacrylamide gel electrophoresis (2-DE). Among the 112 protein spots detected in a silver-stained 2-D polyacrylamide gel, 33 were analyzed by Matrix Assisted Laser Desorption Ionisation tandem time-of-flight mass spectrometry (MALDI TOF/TOF MS), and 21 were identified by MASCOT. There were six structural proteins, such as alpha-actin, tropomyosin, and myosin heavy chain, and six with known functions such as T-cell receptor alpha chain, 4SNc-Tudor domain protein, SMC3 protein, and Translin associated factor X, as well as nine hypothetical novel proteins, including titin, andretinol dehydrogenase, and apolipoprotein A-I binding protein. These proteins were further categorized into six functional groups. This paper established a suitable technical protocol to eliminate the high abundance proteins while preserving middle abundance proteins for proteomics studies using Takifugu skeletal muscle. It is also favorable for further investigation on screening marker proteins for monitoring and controlling the quality of fish meat.
KeywordsTakifugu rubripes Skeletal muscle MALDI TOF/TOF Two-dimensional polyacrylamide gel electrophoresis Proteomics
This work was supported by Natural Science Fund for Colleges and Universities in Jiangsu Province, China (No. 08KJD180008). We thank Professor Yong Wang (Jiangsu University, China) for his revision of our manuscript.
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