The present invention relates to a method for detecting a pathogenic strain having resistance to β-lactam antibiotics in a biological sample, and a method for identifying a protein involved in resistance in β-lactam antibiotics, which is contained in a biological sample. According to the present invention, it is possible to quickly and accurately determine not only whether a pathogenic strain has resistance to antibiotics, but also the type of protein involved in the resistance, by directly identifying an extended spectrum β-lactamase (ESBL) protein with a truncated N-terminus through mass spectrometry. Accordingly, the present invention can be effectively utilized to quickly establish an appropriate antibiotic administration strategy at the initial stage of infection.

The present disclosure provides a profiling method based on comparative mass spectrometry analysis for identifying and quantifying the covalent interactions of electrophilic compounds with diverse proteins in complex proteomes, as well as compositions for performing the method.

A highly sensitive allergen measurement method is provided. A method for detecting an allergen in a sample, comprising: treating a sample with a protease; and detecting presence or absence of an allergen marker in the enzyme-treated sample by analysis that utilizes chromatographic separation. The allergen comprises buckwheat and wheat.

The present disclosure relates to a composition for detecting or measuring an analyte and an analysis method using the composition. In particular, efficiency and performance of sample analysis may be greatly improved through the composition and analysis method of the present disclosure.

A mass spectrometry method comprises: providing a multiplexed sample comprising a mixture of biomolecule-containing samples respectively tagged with mass tags; acquiring MS2 spectra by data-dependent acquisition (DDA) of the multiplexed sample or another mass tagged mixture of the samples during chromatographic elution; acquiring MS2 spectra by data-independent acquisition (DIA) during the elution; forming a spectral library from the DDA MS2 spectra comprising a plurality of the MS2 spectra and the biomolecule retention times; matching fragment-ion peaks in the DIA MS2 spectra to fragment-ion peaks in the MS2 library spectra to find matched biomolecules; determining a total abundance for each matched biomolecule from the DIA MS2 spectra at each of a plurality of retention times; determining abundances of respective reporter ions from the DIA MS2 spectra at the plurality of retention times; and deconvoluting relative abundances of the biomolecules in each respectively tagged biomolecule-containing sample based on the determined abundances.

The present disclosure provides a method for identifying a human growth hormone proteoform (hGHP) pattern biomarker. The method includes: collecting an hGH-secreting pituitary adenoma tissue sample and a normal pituitary tissue sample, and extracting tissue proteins, separately; conducting two-dimensional gel electrophoresis (2DGE), western blotting, and Coomassie brilliant blue (CBB) staining, and scanning visualized polyvinylidene fluoride (PVDF) membranes and 2D gels to obtain digital images; subjecting a corresponding protein in 2D gel spot to protein digestion with trypsin and purification, and conducting mass spectrometry identification and bioinformatics analysis to identify a GHP biomarker profile; and in combination with bioinformatics, using quantitative phosphoproteomics, quantitative ubiquitinomics, and quantitative acetylomics to identify post-translational modifications (PTMs) and splicing variations in GHP. The present disclosure can identify a change pattern of GHP between a GH-secreting pituitary adenoma tissue and a normal pituitary tissue. In total, 46 GHPs are identified in the GH-secreting pituitary adenoma tissue, and only 35 GHPs are identified in the normal pituitary tissue. Therefore, 11 GHPs are only present in the GH-secreting pituitary adenoma tissue.

A method for relative quantification of organic and biological compounds by electrochemical mass spectrometry is disclosed. The method involves using electrochemistry (EC) in a mass spectrometry (MS)-based relative quantitative analysis. In this method, isotope-labeled standards or running calibration curves are not employed. A quantification method could include the steps of subjecting a sample analyte to liquid chromatography or electrophoresis separation, followed by an electrochemical oxidation or reduction in an electrochemical cell, and then mass spectrometric detection.

The present invention relates to method for detecting a free histone protein in a biological sample of a subject, e.g. using an immunoassay or a mass spectrometric assay. It also pertains to a method for the diagnosis, prognosis, risk assessment, risk stratification and/or therapy control of a disease or medical condition, comprising detecting a free histone protein or peptide fragment thereof in a biological sample of a subject, wherein the presence of said free histone protein or fragment thereof is indicative for said disease or medical condition.

A method of mass spectrometry determines if a mutated variant of a target protein is present in a sample. The method includes subjecting the sample to fragmentation so as to cause the target protein to fragment to form second generation fragment ions, and then mass analysing these fragment ions to obtain spectral data. The method determines if a mutated variant is present in the sample by determining that an ion in the spectral data has a mass to charge ratio that differs from the mass to charge ratio of an ion that would be observed if the target protein was a normal unmutated version of the target protein, and by an amount that corresponds to a mass difference that would be caused by the target protein being a mutated variant of the target protein.

The present invention provides: a method of pretreating a serum or plasma sample for detection of a protein or a plurality of proteins of interest in a serum or plasma sample via mass spectrometry and a method of detecting such a protein or proteins, wherein proteins such as albumin present in abundance in a sample are removed in a convenient manner, thereby making it possible to collect digested peptides from the protein of interest. Specifically, the present invention provides a method of pretreating a sample for detecting proteins in a serum or plasma sample via mass spectrometry, comprising a step of adding a protease to the sample under non-denaturing conditions to digest proteins and a step of separating the obtained peptides from undigested proteins, and a method of detecting proteins, comprising subjecting the obtained peptides to mass spectrometry.