1 Proteomics Overview The word "proteome" in English is Proteome, which is a combination of the words proteins and genome, meaning proteins expressed by a genome, which is the protein expressed by the genome [1]. The concept of the proteome was first proposed by Wilkins in 1994 and first published in the July 1995 issue of "Electrophoresis", referring to "all proteins expressed by a cell or a tissue genome" [2], proteomics It is to study the composition and activity of proteins in cells from the overall level. Unlike the gene-fixed genome, the proteome as a product expressed by the corresponding genome changes with time, place, environment and other conditions. In different tissues and different cells of the same body, the types and numbers of proteins are different; even if the same tissue or cells are in different developmental stages, physiological states, or even different external environments, their proteomes are constantly changing; It is also different from normal physiological processes during pathology or treatment. Therefore, the proteome is a dynamic concept. Its purpose is to analyze the dynamic changes of protein composition, expression level, and modification status in the body from a holistic perspective, to understand the interactions and connections between proteins, and to reveal the laws of protein function and life activities. Proteomics research is divided into three aspects: (1) Micro-characteristics of large-scale protein identification and post-transcriptional modification. (2) Differences show that proteomics, the study of protein expression levels, has broad prospects for the application of diseases such as tumors. (3) Studies on protein-protein interactions and post-translational modifications [3]. Analysis of the expression of different proteins can be used to compare the differences between normal and tumor tissues. Proteomics will be a marker for identifying diseases and can illustrate a mechanism that is being applied in more and more analyses. The human genome is much smaller than expected, and the tumor-associated genes in the genome project are now known, whereas smaller genes do not reflect a single proteome. In general, extensive post-translational modifications such as phosphorylation, glycosylation, and proteolytic processing are very common methods. Protein post-translational modifications can significantly alter the function of a protein and thus can express cellular and tissue characteristics. Therefore, one of the challenges of proteomics in the genome is to understand tissue characteristics through knowledge of protein effectors and apply it to the clinic. 2 proteomics analysis method Proteomics can be analyzed by protein microarrays, electrophoresis and mass spectrometry for detection, identification and signature of proteins. These methods have their unique advantages and limitations, and the proteomic profiles are evaluated according to their respective abilities. 2.1 protein micro-column technology The protein microcolumn is a test for the analysis of a large number of antibodies or a large amount of tissue protein samples on a glass slide at a time. This method is capable of detecting the presence of large amounts of protein or the level of expression of a large number of tissue samples, but this technique is limited in the availability of specific and sensitive antibodies. Furthermore, the specificity of the antibody must be confirmed by immunoblotting and requires an internal control, especially the microarray of the antibody has no predicted affinity and specificity. Despite this, the use of a large number of commercially available antibodies makes it possible to apply protein microarrays. 2.2 Two-dimensional gel electrophoresis Two-dimensional electrophoresis was invented by O'Farrell in 1975. The principle is that the first-direction protein-based isoelectric point is different and is separated by isoelectric focusing. The second direction is different by molecular mass using sodium lauryl sulfate-polymerization. Acrylamide gels separate proteins in complex protein mixtures on a two-dimensional plane. This method is especially useful for proteins with similar molecular weights. Using a proteome contig, using multiple 2-DE maps with different pH gradients and overlapping molecular weights, splicing into a complete 2-DE map, greatly improving resolution and injection volume, which is useful for low-abundance proteins. Checking out is very beneficial. Individual proteins can be stained and hydrolyzed into peptides, which can be analyzed by mass spectrometry. The enzymatic map of the peptide can be analyzed from a database of proteins. 2.3 Mass spectrometry One of the main tools of proteomics is mass spectrometry. In this method, after the gene is converted into a gas ion, the protein is analyzed according to the ratio of the feed. Solubilization and ionization techniques such as matrix-assisted laser desorption ionization provide a high level of sensitivity and precision for the detection and resolution of proteins. The high sensitivity of this technology and the simplification of the sample make this technology convenient. , but it also has limitations. Analysis of complex samples such as serum is much more difficult than detecting proteins.
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