The invention relates to a method for the determination and visualization of the spatial distribution of tissue states of a tissue sample, wherein a mass/mobility map is acquired at each of a plurality of sample sites of the tissue sample, the signal heights at each sample site are determined at characteristic signal positions in the corresponding mass/mobility map, from which a tissue state for each sample site is calculated with the aid of a mathematical/statistical classification algorithm, and the spatial distribution of the tissue states calculated for the sample sites is represented graphically.

This disclosure relates to new methods for antibody characterization sequencing, such as middle down antibody characterization and sequencing, for example, for de novo antibody sequencing, identifying known antibodies in a sample, or verifying the sequence of antibodies in a sample. In some embodiments, the methods involve exposing antibodies to cathepsin D, cathepsin L, and/or cathepsin D and L, followed by mass spectrometry and sequence identification and deconvolution.

The invention provides a method for detecting one or more analytes, the method comprising: providing a substrate comprising a semiconductor with a porous surface, wherein the porous surface is coated with a fluorocarbon polymeric coating; contacting the porous surface with a fluid or object so that the one or more analytes are retained on the substrate when present in the fluid or on the object; and analysing the substrate by mass spectrometry to detect the one or more analytes if present on the substrate.

To provide a method for discriminating a microorganism by selecting and using a marker protein capable of reproducibly and quickly discriminating a bacterial species of the genus Listeria. The method for discriminating a microorganism according to the present invention includes: a step of subjecting a sample containing a microorganism to mass spectrometry to obtain a mass spectrum; a reading step of reading a mass-to-charge ratio m/z of a peak derived from a marker protein from the mass spectrum; and a discrimination step of discriminating which bacterial species of Listeria bacteria the microorganism contained in the sample contains based on the mass-to-charge ratio m/z, in which at least one of 17 ribosomal proteins L3, L4, L23, L2, L24, L6, L18, S5, L15, S13, S11, L10, L21, L13, S9, L31, S16 is used as the marker protein and particularly at least one of 8 ribosomal proteins L24, L6, L18, L15, S9, L31, S16 among the 17 ribosomal proteins is used.

A biomarker diagnostic system includes a sensor to collect a sweat sample from a biological subject; a processor operatively connected to the sensor, wherein the processor is configured to perform metabolic and proteomic profiling of biomarkers in the sweat sample. The metabolic and proteomic profile is compared to a predetermined profile of the biomarkers and to determine a physiological status of the biomarkers. The system further includes a feedback unit operatively coupled to the sensor and the processor and configured to output physiological performance data based on the physiological status.

A method for characterizing or quantifying one or more proteins in visible and/or sub-visible particles formed in a sample by detecting the at least one visible or sub-visible particle in the sample, isolating and capturing the at least one visible or sub-visible particle to identify a presence of a protein, and using a mass spectrometer to characterize the protein.

The present invention provides a snake venom thrombin marker peptide of Agkistrodon Halys Pallas and an application of the snake venom thrombin-like enzyme in identifying species of Hemocoagulase for Injection. The application includes the following steps of: dissolving a to-be-detected sample and a reference substance of the marker peptide respectively to prepare a test solution and a reference solution, and conducting alkylation reduction on the test solution and the reference solution with dithiothreitol and iodoacetamide; after diluting products with an ammonium bicarbonate solution, adding enzyme for hydrolysis; and after enzymolysis is finished, conducting centrifugation at a high speed, and injecting a supernatan into a liquid chromatography-mass spectrometer for analysis. This method is simple, convenient and rapid, is strong in specificity, fills the gap in identifying the source of species of the snake venom thrombin-like enzyme of Agkistrodon Halys Pallas and improves the quality control level.

Methods of assessing an analyte in a blood sample are provided according to aspects of the present disclosure which include: extracting the analyte from a biological sample dried on a treated support, producing an extracted sample, the treated support comprising a protein denaturant, wherein the analyte is a substrate for an enzyme present, or suspected of being present, in the biological sample, wherein the protein denaturant inhibits enzymatic activity of the enzyme on the analyte; and subjecting the extracted sample to liquid chromatography tandem mass spectrometry (LC/MS/MS), thereby assessing the analyte in the biological sample.

The present disclosure relates to novel and improved methods of analyzing proteins, peptides and polypeptides by mass spectrometry using ion-ion reactions. More specifically the disclosure relates to improved methods for implementing the m/z selective arresting of ion-ion reactions within the ion-ion reaction cell of a mass spectrometer system during a period where ion-ion reactions are performed.

Methods and systems directed to monitoring for the presence or progression of amyloid diseases via detection of amyloid fibrils in a sample from an individual are disclosed. An individual, or sample from an individual, is treated with a reagent including a fluorescent protein. The fluorescent protein in the reagent binds to amyloid fibrils present in the sample. Detecting a signal from fluorescent protein bound to the treated sample indicates the presence of amyloid fibrils in the sample and possible diagnosis of an amyloid disease. The presence and progression of an amyloid disease is monitored by quantifying signal intensity from samples taken over time. Treatment with a reagent including a fluorescent protein inhibits amyloid fibril formation by providing the reagent to an environment including amyloid monomers. The fluorescent protein binds to amyloid oligomers during the lag phase and/or elongation phase of amyloid fibril formation, preventing formation of mature amyloid fibrils.