A method of analysis using mass spectrometry and/or ion mobility spectrometry is disclosed comprising: (a) using a first device to generate smoke, aerosol or vapour from a target plant material; (b) mass analysing and/or ion mobility analysing said smoke, aerosol or vapour, or ions derived therefrom, in order to obtain spectrometric data; and (c) analysing said spectrometric data in order to identify and/or characterise said plant material.

The present disclosure relates to a method of characterizing proteins in a sample. The method includes: removing non-ionic surfactant from the sample via denaturing size-exclusion chromatography to form a denatured sample; eluting the denatured sample via liquid chromatography to collect fractions of the sample, wherein the fractions of the sample include a protein fraction; lyophilizing the protein fraction to increase protein concentration; reconstituting the lyophilized protein fraction with a buffer comprising a surfactant to denature the protein; digesting the denatured protein fraction with an enzyme; and analyzing the digested protein fraction.

A method of analysis using mass spectrometry and/or ion mobility spectrometry is disclosed comprising: (a) using a first device to generate smoke, aerosol or vapour from a target in vitro or ex vivo cell population; (b) mass analysing and/or ion mobility analysing said smoke, aerosol or vapour, or ions derived therefrom, in order to obtain spectrometric data; and (c) analysing said spectrometric data in order to identify and/or characterise said target cell population or one or more cells and/or compounds present in said target cell population.

The invention relates to the quantitative measurement of steroidal compounds by mass spectrometry. In a particular aspect, the invention relates to methods for quantitative measurement of steroidal compounds from multiple samples by mass spectrometry.

The method describes rapid screening of whole blood samples, pin prick and blood spot cards, subjected to MALDI-ToF Mass spectrometry. The spectra is generated and compared to those from normal healthy controls. Characteristic spectra are indicative of the presence of a hemoglobinopathy and the method can be used to screen/diagnose all sickle cell diseases, alpha and beta Thalassemias.

Disclosed are components, systems, and methods for glycoprotein or recombinant glycoprotein protein synthesis in vitro and in vivo. In particular, the present invention relates to components, systems, and methods for identifying amino acid glycosylation tag motifs for N-glycosyltransferases and the use of the identified amino acid glycosylation tag motifs in methods for preparing glycoproteins and recombinant glycoproteins in vitro and in vivo.

The invention proposes preparing biological samples for spectrometry which contain cell structures and/or whole cells of human or animal origin (e.g. thin human and animal tissue sections) or prokaryotes (e.g. microorganisms), and which require constant relative humidity, in a temperature-controlled gas volume whose humidity is determined by a saturated substance solution, for example a suitable salt solution. The invention exploits a physico-chemical phenomenon called “deliquescence”, which manifests itself by keeping the relative humidity above the saturated substance solution constant with a high degree of precision when a specified temperature is maintained. Pure succinic acid exhibits deliquescence at approx. 99% relative humidity, for example. Since an enormous variety of deliquescent salts and other suitable substances are available, it is possible to find the suitable substance for almost any desired relative humidity, with adjustment of the temperature, where necessary.

The invention generally relates to high-throughput label-free enzymatic bioassays using desorption electrospray ionization-mass spectrometry (DESI-MS).

Disclosed is a method for measuring an Aβ peptide, comprising: mixing a blood sample comprising an Aβ peptide and an antibody that specifically binds to the Aβ peptide to form a complex of the Aβ peptide and the antibody; releasing the AP peptide from the complex with a basic solution comprising an organic solvent; and measuring the released Aβ peptide by mass spectrometry.

A surface-assisted laser desorption/ionization method according to an aspect includes: a first process of preparing a sample support (2) having a substrate (21) in which a plurality of through-holes (S) passing from one surface (21a) thereof to the other surface (21b) thereof are provided and a conductive layer (23) that covers at least the one surface (21a); a second process of placing a sample (10) on a sample stage (1) and arranging the sample support (2) on the sample (10) such that the other surface (21b) faces the sample (10); and a third process of applying a laser beam (L) to the one surface (21a) and ionizing the sample (10) moved from the other surface (21b) side to the one surface (21a) side via the through-holes (S) due to a capillary phenomenon.