Rice proteomics: improved peptide mapping and its application to identification of the embryo proteins
2001
Wo, S. | Fukuda, H. | Takaoka, M. | Kawasaki, H. | Hirano, H. (Yokohama City Univ., Yokohama (Japan). Kihara Inst. for Biological Research)
Western blotting/sequencing techniques has come to be widely used in protein sequence analysis. However, the N-terminally blocked proteins cannot be sequenced by the blotting/sequencing technique. In the proteome analysis of rice approximately 700 embryo proteins were separated by two-dimentional gel electrophoresis (2-DE) and the N-terminal sequences of approximately 100 embryo proteins were analyzed by the blotting/sequencing technique. In this analysis, it was found that many proteins (69%) were N-terminally blocked. Thus, a simple and rapid method for obtaining sequence information on the blocked proteins should be developed. The Cleveland peptide mapping was improved to determine the internal amino-acid sequences of proteins including the N-terminally blocked proteins. By the use of this method, the peptide maps of 100 proteins could be obtained for 10 days. Among the 100 proteins, 47 showed sequence similarity to the proteins with known functions in the SWISS-PROT database. Alternatively, peptide mass fingerprinting by MALDTOF/MS was used to identify the rice embryo proteins separated by 2-DE. This method allows high-throughput analysis, but not always easy identification of the rice embryo proteins or gene. Because in rice, the complete database has not been available and many proteins are post-translationally modified. Therefore, at present, the improved peptide mapping is considered to be useful in the rice proteome analysis
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