家蚕30k蛋白的结构功能及五龄血浆蛋白质组学分析-structural function of silkworm 30k protein and proteomic analysis of 5th instar plasma.docx
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家蚕30k蛋白的结构功能及五龄血浆蛋白质组学分析-structural function of silkworm 30k protein and proteomic analysis of 5th instar plasma
Abstract
Abstract
IV
IV
molecular function of this protein.
The completion of the B. mori genome sequences made it possible to understand the information between gene expression and function and the proteomic analysis can be actualized through this database. To improve the understanding of this important bioprocess and gene expression situation, we utilized the proteomic approach to investigate the proteome of the fifth instar hemolymph during growth and development. The One-Dimensional gradient acrylamide SDSElectrophoresis method (1D-SDS) in gel digestion and the different pH values of hemolymph in solution digestion, combination with the Two Dimensional Liquid Chromatography Electrospray Ionization Tandem-Mass Spectrometry (2DLC-MS) technique were used here to analyze the proteome of the hemolymph of the Bombyx mori in 5th instar. In total, 289 proteins are identified; the isoelectric point values of these proteins range from 4–12. Most of the proteins are soluble in water, have a molecular weight of 10–60 kDa. The functions of these identified proteins were categorized by NCBI BLAST and Gene Ontology. These proteins belong to 12 functional categories and most of them involved in storage, defense, transport and metabolism. Furthermore, the levels of expression of 30K proteins were investigated. The results showed that its highest expression was reached at the early of the pupa stage, then disappeared in hemolymph of both sex moths, and the expression level correlates well with their functions. The results of the hemolymph proteomics will help us for the future study of these ‘hot spot’ proteins.
Key Words: Silkworm, crystal structure, 30K proteins, β-trefoil superfamily, sugar-binding site, hemolymph, proteome
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