The present invention relates to a method for detecting a pathogenic strain having resistance to carbapenem antibiotics in a biological sample. According to the present invention, it is possible to directly identify carbapenemases, specifically KPC, OXA, NDM, IMP, VIM and/or GES protein, by mass spectrometry, thereby making it possible to quickly determine not only whether a pathogenic strain has resistance to antibiotics, but also the type of protein involved in the resistance. According to the present invention, the physical and chemical properties of each carbapenemase in vivo, such as the unique N-terminal truncation length, methionine residue oxidation and disulfide bond formation in each type of carbapenemase, are identified and are reflected on reference mass values. Accordingly, it is possible to more closely detect the presence of an antibiotic-resistant strain with high reliability, and thus the present invention may be advantageously used to establish an appropriate strategy for antibiotic administration at an early stage of infection.

A chromatographic testing device which is configured to select an imaging scheme according to the type of fluorescent dye in an immunochromatographic test cartridge and a method for controlling the same are disclosed. The chromatographic testing device can include: a body; a code expression recognition unit provided in the body and recognizing a code expression in which a type of fluorescent dye of an immune strip provided on an immunochromatographic test cartridge mounted on the body is recorded; an excitation light source emission unit for emitting light from an excitation light source to the immunochromatographic test cartridge; an image sensor unit for recognizing excitation light generated by the excitation light source; and a control unit for controlling the image sensor unit in a single imaging scheme or a cumulative light imaging scheme according to the type of fluorescent dye of an immune strip, recognized by the code expression recognition unit.

The current invention is based, at least in part, on the finding that the transverse nuclear magnetic spin relaxation time T2 and the transverse nuclear magnetic spin relaxation rate R2, respectively, of protons of water molecules in an aqueous solution comprising viral particles depends on the loading status (full vs. empty) of the viral particle. Thus, one aspect of the current invention is a method for determining the ratio of loaded viral particles to empty viral particles in a sample, comprising the steps of determining a nuclear magnetic resonance (NMR) parameter related to the protons of the water molecules present in an aqueous solution comprising a mixture of loaded and empty viral particles by applying an NMR measurement to the solution, and determining the ratio of loaded viral particles to empty viral particles with the NMR parameter determined in the previous step based on a calibration function.

The present invention belongs to the technical field of metabolomics, and relates to a metabolomics relative quantitative analysis method based on UPLC/HRMS. Specifically, the present method mainly comprises the steps of formulating an isotope internal standard mixed solution, a standard curve correction solution, and a metabolomics sample solution; acquiring raw mass spectrum data of the standard curve correction solution and the metabolomics sample solution; transposing and deconvolving the raw data; identifying and selecting the optimal isotope internal standard; fitting a linear equation and calculating the relative quantitative results of metabolites in the metabolomics sample solution; and completing the structural identification of metabolites and differential metabolites in the metabolomics sample solution. The method can meet both qualitative and quantitative requirements using only a high-resolution mass spectrometry platform; the quantitative results are accurate, and the accuracy of the qualitative results are higher, having low costs, simple operation, and wide applicability.

A method for determining a quantity of an analyte in a liquid sample, comprises: adding a known quantity of an internal standard comprising an isotopically labeled version of the analyte to the sample; (b) providing a continuous stream of the sample having the internal standard to an inlet of a Liquid Chromatography Mass Spectrometry (LCMS) system; and repeatedly performing the steps of: performing a data-independent analysis of the precursor ion species using a mass analyzer, whereby mass spectra of a plurality of fragment-ion species are acquired; calculating one or more degree-of-matching scores that relate to either a number of ions of the internal standard that overlap between results of the data-independent analysis and tabulated mass spectral data of the internal standard; and performing quantitative tandem mass spectrometric analyses of the internal standard and the analyte if each of the degree-of-matching scores meets a respective degree-of-matching condition.

The present invention relates to the field of protein characterization, and in particular to methods for identifying critical quality attributes of therapeutic proteins by implementing a workflow including using a competitive binding assay with insufficient capture molecule followed by LC-MS.

Methods and system for identifying and quantifying antibody fragments and identifying the site of fragmentation on an antibody are provided herein.

Described herein are methods for evaluating polymer compositions comprising polymers modified with a polypeptide (e.g., a cell-binding polypeptide), including methods for determining polypeptide concentration.

The present invention generally pertains to methods of characterizing at least one protein of interest in a biological sample. In particular, the present invention pertains to the use of automated iterative tandem mass spectrometry (AIMS) to identify, quantify and characterize at least one protein of interest and/or biomarker from a biological sample such as plasma.

The present disclosure discusses a method of separating a sample of tyrosine kinase inhibitors or metabolites of tyrosine kinase inhibitors which includes injecting the sample into the chromatographic system having one or more low-bind coated surfaces along the flow path; flowing the sample through the chromatographic system; separating the sample; and analyzing the separated sample. Consequently, the sample does not bind to the low-binding surface coatings (e.g., alkylsilyl coatings) of the flow path. The applied coating can reduce peak tailing and decrease carryover for tyrosine kinase inhibitor samples during chromatographic analysis.