Patents
Literature
Patsnap Copilot is an intelligent assistant for R&D personnel, combined with Patent DNA, to facilitate innovative research.
Patsnap Copilot

85 results about "Maldi ms" patented technology

Application of naphthylethylenediamine inorganic acid salt or Naphthylethylenediamine organic acid salt as matrix in MALDI MS (matrix-assisted laser desorption/ionization mass spectrometry)

The invention discloses application of naphthylethylenediamine inorganic acid salt or naphthylethylenediamine organic acid salt as a matrix in MALDI MS (matrix-assisted laser desorption/ionization mass spectrometry). In the application, the MALDI MS is MALDI-TOF MS (matrix-assisted laser desorption/ionization - time-of-flight mass spectrometry); the naphthylethylenediamine inorganic acid salt is naphthylethylenediamine hydrochloride, naphthylethylenediamine nitrate, naphthylethylenediamine phosphate or naphthylethylenediamine sulfate; and the naphthylethylenediamine organic acid salt is naphthylethylenediamine trifluoroacetate, naphthylethylenediamine acetate, naphthylethylenediamine formate, naphthylethylenediamine citrate or naphthylethylenediamine oxalate. The invention technically overcomes the defect that small-molecule samples cannot be effectively analyzed because serious matrix background interference is apt to be caused in a low molecular weight zone when organic small-molecule matrices are commonly used. The matrix used by the invention is not required to be added with ionizing reagent and the requirements on sample treatment are reduced; and since background interference hardly exists within a testing range (m/z: 0-1000), kinds of complex mixed systems can also be analyzed by using the matrix.
Owner:INST OF CHEM CHINESE ACAD OF SCI

Application of naphthylhydrazine inorganic acid salt or Naphthylhydrazine organic acid salt as matrix in MALDI MS (matrix-assisted laser desorption/ionization mass spectrometry)

The invention discloses application of naphthylhydrazine inorganic acid salt or naphthylhydrazine organic acid salt as a matrix in MALDI MS (matrix-assisted laser desorption/ionization mass spectrometry). The MALDI MS is MALDI-TOF MS (matrix-assisted laser desorption/ionization - time-of-flight mass spectrometry); the naphthylhydrazine inorganic acid salt is naphthylhydrazine hydrochloride, naphthylhydrazine nitrate, naphthylhydrazine phosphate or naphthylhydrazine sulfate; and the naphthylhydrazine organic acid salt is naphthylhydrazine trifluoroacetate, naphthylhydrazine acetate, naphthylhydrazine formate, naphthylhydrazine citrate or naphthylhydrazine oxalate; and hydrazine radicals on the naphthylhydrazine inorganic acid salt or naphthylhydrazine organic acid salt are all 1-substituted or 2-substituted. The application technically overcomes the defect that small-molecule samples cannot be effectively analyzed because serious matrix background interference is apt to be caused in a low molecular weight zone when organic small-molecule matrices are commonly used. The matrix used by the invention is not required to be added with ionizing reagent and the requirements on sample treatment are reduced; and since background interference hardly exists when m/z is smaller than 500, various complex mixed systems can also be analyzed by using the matrix.
Owner:INST OF CHEM CHINESE ACAD OF SCI

Quantitative, high-throughput screening method for protein stability

In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described herein are methods (referred to as MALDI MS-HX and SUPREX) for measuring the stability of proteins in a rapid, high-throughput fashion. The method employs hydrogen exchange to estimate the stability of quantities of unpurified protein extracts, using matrix-assisted laser desorption / ionization (MALDI) mass spectrometry. A method of quantitatively determining the stability of a test protein under native conditions is disclosed. The method includes the steps (a) providing a test protein; (b) contacting the protein with an exchange buffer comprising a denaturant and deuterium, the exchange buffer having a denaturant concentration; (c) contacting the test protein with a mass spectrometry matrix medium; (d) determining a change in mass of the test protein by mass spectrometry; (e) varying the denaturant concentration of the exchange buffer; (f) repeating steps (a)-(e) a desired number of times; and (g) quantitatively determining protein stability based on the change in mass of the test protein as a function of denaturant concentration, whereby the stability of a test protein under native conditions is quantitatively determined.
Owner:DUKE UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products