A system and method for chemical analysis are described herein. The system includes a probe, a sample collection cartridge, and a chemical analyzer. The probe is configured to collect the optimal amount of sample for a future analysis and to store this chemical sample in the sample collection cartridge. The probe also collects sample data. The chemical analyzer is configured to determine the optimal analysis settings based on the sample data and analyze the chemical sample stored in the sample collection cartridge based on the optimal analysis settings.

The present invention relates to the technical field of chemical analysis and quantitative detection, in particular to a quantitative detection method for snake venom thrombin-like enzyme (SVTLE) from Agkistrodon halys pallas. The quantitative detection method for the SVTLE includes the following steps of taking a reference substance of marker peptide for the SVTLE from Agkistrodon halys pallas with an amino acid sequence of LDSPVSNSAHIAPLSLPSSAPSVGSVCR, and preparing a series of reference solutions with different concentrations; adding the reference solutions in test solutions respectively for enzymolysis, and then taking a supernatant after enzymolysis as a series of solutions to be detected; and adding the solutions to be detected in a liquid chromatogram-mass spectrometer, and then selecting a qualitative ion pair and a quantitative ion pair to detect contents of marker peptide in the solutions to be detected.

The present invention relates to the field of chemical analysis detection and application, in particular to a marker peptide of snake venom thrombin-like enzymes (SVTLEs) from Agkistrodon Halys Pallas and an application thereof. The amino acid sequence of the marker peptide of snake venom thrombin-like enzymes (SVTLEs) from Agkistrodon Halys Pallas is TLCAGVMEGGIDTCNR. Characterizing the source of species and a content of the SVTLEs in a to-be-detected sample by using the marker peptide includes the following steps of: pretreating the to-be-detected sample by trypsin through enzymolysis, and taking a supernatant of an enzymolysis liquid as a test solution; and injecting the test solution and a reference solution into a liquid chromatography-mass spectrometer, and selecting a qualitative ion pair and a quantitative ion pair for detecting the source of species and a content of the SVTLEs in the to-be-detected sample.

Provided is a method for detecting impurities in ammonium hydroxide. The method for detecting impurities in ammonium hydroxide includes preparing a potassium permanganate solution, preparing ammonium hydroxide, and adding the potassium permanganate solution several times to the ammonium hydroxide so as to detect impurities in the ammonium hydroxide. Potassium permanganate contained in the potassium permanganate solution is added for each time in the range of 0.0001 mol to 0.01 mol per 1 g of ammonia contained in the ammonium hydroxide.

The present invention relates to a method for quantitatively analyzing Cl, remaining after synthesis, in zinc ferrite synthesized using chloride precursors such as zinc chloride and iron chloride, and provides a method capable of using, in a quantitative analysis method of Cl remaining after synthesis of an inorganic material, AQF-IC, which has been used only in the quantitative analysis of an organic sample since gaseous Cl, discharged after burning zinc ferrite in an automatic quick furnace (AQF) by using an Sn capsule and tungsten oxide (WO3), is analyzed through ion chromatography (IC).

Techniques disclosed herein can be used to perform a rapid, splitless injection of a sample including SVOCs and VOCs. In some embodiments, a system includes two focusing traps combined in series, one inside of a GC oven and one in a separate oven to concentrate the SVOCs inside of the GC oven and concentrate the VOCs outside of the GC oven. Heating the VOC focusing trap and reversing the flow through both focusers allows splitless injection of compounds boiling from as low as −100° C. to as high as 600° C. in a single analysis, with a narrow injection bandwidth to optimize both sensitivity and the resolving power of the analyzer.

The present invention provides a method for detecting a monoclonal antibody in a sample, the method comprising: (a) a step of capturing and immobilizing, in pores of a porous body, the monoclonal antibody in the sample; (b) a step of performing selective protease digestion of the monoclonal antibody for 30 min or longer by contacting the porous body having the monoclonal antibody immobilized thereon with nanoparticles having a protease immobilized thereon; and (c) a step of detecting a peptide fragment obtained by the selective protease digestion, using liquid chromatography mass spectrometry (LC-MS), wherein step (b) is carried out under stirring condition for 10 sec to 5 min in the initial reaction stage, and then under static condition. According to the present invention, the detection method of a monoclonal antibody using mass spectrometry is simplified and can be applicable to multisample analysis.

The present invention provides a method for detecting a monoclonal antibody in a sample, the method comprising: (a) a step of capturing and immobilizing, in pores of a porous body, the monoclonal antibody in the sample; (b) a step of performing selective protease digestion of the monoclonal antibody for 30 min or longer by contacting the porous body having the monoclonal antibody immobilized thereon with nanoparticles having a protease immobilized thereon; and (c) a step of detecting a peptide fragment obtained by the selective protease digestion, using liquid chromatography mass spectrometry (LC-MS), wherein step (b) is carried out under stirring condition for 10 sec to 5 min in the initial reaction stage, and then under static condition. According to the present invention, the detection method of a monoclonal antibody using mass spectrometry is simplified and can be applicable to multisample analysis.

Disclosed are methods for identification of one or more non-native disulfide bonds in a biomolecule (e.g, an antibody). In an example, a method includes performing a digestion of the biomolecule under non-reducing conditions to provide a sample comprising a plurality of biomolecule fragments, contacting the sample to a separation column, applying a first mobile phase gradient comprising trifluoroacetic acid (TFA) and a small molecule additive to the separation column, applying a second mobile phase gradient comprising TFA in acetonitrile (ACN) and a small molecule additive to the separation column, performing a partial reduction procedure on the eluted sample, applying the partially reduced eluted sample components to a mass spectrometer, and performing a mass spectrometric analysis on the partially reduced eluted sample components to identify the one or more non-native disulfide bonds in the biomolecule.

The invention relates to a method for the treatment of body fluid proteins, by which proteins from body fluids such as blood or urine are extracted by adding a certain proportion of high molecular polymer solution under low temperature condition followed by denaturation and reduction by adding a certain concentration of surfactant and tris(2-carboxyethyl) phosphine (TCEP) under a high temperature condition. Subsequently, the iodoacetic acid brushes grafted on silica microspheres called as solid-phase alkylation reagents are added into protein solution, which can react rapidly with the protein sulfhydryl group. After centrifugation, the microspheres are obtained and repeatedly washed with methanol and buffer to remove interferences such as sugars, salts, surfactants, lipids to obtain high-purity proteins, and finally protease is added to digest proteins into peptides. After centrifugation, the peptide products are obtained, and directly analyzed by liquid chromatography-mass spectrometry (LC-MS) system. Compared with the traditional protein pretreatment method, the method has many advantages such as good anti-interference capability, easy operation and short pretreatment time.