A rapid processing method for phosphorylated proteome samples

A technology for phosphorylating proteins and processing methods, applied in the preparation of test samples, etc., can solve the problems of high non-specific adsorption performance of immobilized enzymes, inconvenient operation, and no generalization, and achieve high-quality spectral identification coverage. Effect
CN104949864BInactive Publication Date: 2017-12-05DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
Publication Date
2017-12-05
Estimated Expiration
Not applicable · inactive patent

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Abstract

The present invention relates to a rapid processing method for phosphorylated proteome samples. Utilizing the advantage that high-concentration trypsin can promote rapid enzymatic hydrolysis of proteins, a new type of sample processing method integrating cell lysis and proteolysis is developed, and its Applied to the analysis of phosphoproteomics. Thanks to the deep mechanism of simultaneous cell lysis and proteolysis promoted by the high concentration of trypsin, the cell sample can be rapidly converted into a peptide mixture in a single step. During the enrichment of phosphopeptides, non-phosphorylated peptides As well as various other mass spectrometrically incompatible impurities, can be removed. The present invention only needs 25 minutes to realize the rapid transition from cells to peptides, and in the normal control group, the simplest method also needs at least 16 hours; The excellent coverage of mass spectrum identification proves the accuracy and efficiency of this sample pretreatment method.
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Description

technical field

[0001] The invention belongs to the technical field of phosphoproteomics in the direction of proteomics research, and specifically relates to a sample processing method applied to phosphoproteomics. Background technique

[0002] To date, protein phosphorylation has been found to be a ubiquitous protein post-translational modification that regulates approximately 30% of the eukaryotic proteome. As an important post-translational modification, reversible protein phosphorylation plays an important role in the regulation of cell metabolism, such as cell differentiation, cell proliferation, cell apoptosis and signal transduction, etc. Various intracellular and extracellular stimuli can cause abnormal changes in intracellular phosphorylation levels, and this is precisely the cause of many human diseases. Therefore, in order to systematically understand the complex and variable cellular behavior, in-depth study of the phosphoproteome has become a key task. Recentl...

Claims

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