The principle of biomass spectrum technology and its application and prospect.

Life Sciences is regarded as one of the most cutting-edge science in the 21st century, with the completion and development of the first human gene sequence sketch, life science research will also enter a new era of post
genomics
, that is,
protein
histology.
just as the early mapping of genetic sketches has benefited from large-scale fully automatic capillary sequencing technology, post-genome research will also be rapidly developed with the help of modern biological
meteorum spectrometry
technology. This paper intends to briefly describe biomass spectrum technology and its application in the field of life science.1 Mass SpectrometryMass Mass Mass Spectrometry is a map of charged atoms, molecules, or molecular fragments in order of mass-to-mass ratio (or mass).
mass spectrometer is a class of instruments that can make matter particles high into ions and achieve mass-to-load ratio separation by spatial position, time seism, or orbital stability through an appropriate electric field and magnetic field. Mass spectrometers are mainly composed of analytical systems, electrical systems and vacuum systems.Basic principles of mass spectrometrography Sample molecules (or atoms) used for analysis are ionized into single-line molecular ions and fragmented ions with different mass in the ion source, which obtain the same momentum and form a beam of ions in the accelerated electric field, and enter an analyzer composed of electric and magnetic fields, where slower ions are converted through the electrocfield and defleter is small;
In the magnetic field, the ions have the opposite deflegment of the angle velocity vector, i.e. the slow ions are still deflected large and the rapid deflegation is small;
At the same time, mass separation can also occur in the magnetic field, so that ions with the same mass-to-load ratio and different velocity are focused on the same point, the ions of different mass-to-load ratios are focused on different points, their focal surface is close to the plane, where the spectral line of different mass-to-load ratios can be obtained by testing the detection system, i.e. mass spectromet.
mass spectrometrometrography, we can obtain information on molecular weight, molecular form, isotope composition and molecular structure of the analysis sample.the development ofmass spectrometrometromety dates back to the parabola mass spectrometrometer created by J.J. Thomson in the early 20th century, and in 1919 Aston made the first speed-focused mass spectrometer, becoming a milestone in the history of mass spectrometography.'s original mass spectrometer was mainly used to determine the atomic weight of elements or isotopes, with the development of ion optical theory, mass spectrometers continue to improve, its application range is also expanding, to the late 1950s has been widely used in inorganic compounds and organic compounds determination.today, mass spectrometrometography has been used in various fields of technology, including solid physics, metallurgy, electronics, aerospace, atomic energy, earth and cosmical chemistry,
biochemistry
and life sciences. The application of mass spectrometrometromet technology in the field of life science has injected new vitality into the development of mass spectrometrography and formed a unique biomass spectromet technology.
2 Biomass Spectrometrography .Electrosal spray mass spectrometry and substring-assisted laser desorption mass spectrometry were two rail ion ion technologys born in the late 1980s. The emergence of these two technologies has revolutioned the traditional mass spectrometrography technology, which is mainly used for the study of small molecular substances.
They have a high sensitivity and high-quality detection range, making it possible to accurately analyze biomol molecules with molecular weights of tens to hundreds of thousands of molecules at pmol (10-12 or even fmol (10-15 levels) so that mass spectrometrometrometromet technology can truly enter the field of life science research and develop rapidly. The following mainly describes
mass spectrometromet
related to biomedical and biomedical research.electrospray mass spectrometry technologyelectrospray Mass Spectrometry (ESI-MS) is the application of a high voltage at the outlet of the capillary tube, resulting in a high electric field that flows from the capillary tube The liquid atomizes into a small charged droplet, and as the solvent evaporates, the charge strength of the surface of the droplet gradually increases, and finally the droplet disintegates into a large number of ions with one or more charges, causing the admiss to enter the gas phase in the form of a single charge or multi-charged ion.
electrosurger ionization is characterized by the generation of high charge ions rather than fragmented ions, so that the mass charge ratio (m/z) is reduced to the range that most mass analysis instruments can detect, thus greatly expanding the range of molecular weight analysis, the true molecular mass of ions can also be calculated according to the mass ratio and the number of lines.advantage of electrosurfuring mass spectrometrometrometrography is that it can be easily used in combination with a variety of separation technologies, such as liquid-ion combination (LC-MS) is the liquid phase
chromat spectrometrometrometrography
and mass spectrometrometrometrography to achieve the purpose of detecting large molecular substances.matrix-assisted laser desorption mass spectrometry technologymatrix-assisted laser desorption mass spectrometry technology (MatriX Assisted Laser Desorption /Ionization, MALDI) is based on the principle of Dispersed in the substring molecules and the formation of crystals, when the laser is used to irradiate the crystal, due to the energy absorbed by the substate molecules by radiation, resulting in energy accumulation and rapid heat production, so that the substring crystal sublimation, resulting in the expansion of the substate and analyte into the gas phase.
the mass spectrogram produced by MALDAI is mostly single-charged ions, so the ions in the mass spectrometography are related to the quality of
polypeptides
and proteins..MALDI-produced ions are often detected by time-of-flight (Time-flight, TOF) detectors, which theoretically have no upper limit on the mass of molecules that can be detected by the TOF detector as long as the length of the flight tube is sufficient, so the MALDI-TOF mass spectrometry is well suited for the study of biological large molecules such as proteins, peptides, nucleic acids and polysaccharides.Fast Atomic Bombardment Mass Spectrometry TechnologyFast Atom Bomebard-ment Mass Spectrometry (FABMS) is a soft ionization technique that uses fast inert atoms to shoot samples found in the substrate, allowing sample ions to spill into the analyzer, which is suitable for the analysis of extremely strong, thermally unstable compounds, and is specific to the analysis of polypeptides and proteins..FABMS can only provide precise mass of ions, allowing the elemental composition and molecular form of the sample to be determined. The application of FABMS-MS series technology can provide more detailed molecular structure information of the sample, which makes it develop rapidly in biomedical analysis.iso-quality spectrum is a relatively early development and application of technology, widely used in various fields, but its application in the field of medicine is only in recent years. Because some pathogens have the ability to break down specific compounds, the compound is easy to be labeled with isotopes, people think of using isotope quality spectrum method to detect the content of isotopes in their metabolites to achieve the purpose of detecting the pathogen, but also for the application of isotope quality spectrum in the medical field opened up a way of thinking.
3 Biomass Spectrum Technology .With the continuous improvement and perfection of mass spectrometry technology, the application scope of mass spectrometry has been extended to many fields of life science research, especially the application of mass spectrometry in protein, medical testing, drug composition analysis and nucleic acid, which not only provides new methods for life science research, but also promotes the development of mass spectrometry technology.mass spectrometry and protein analysisprotein molecular weight determination protein biometric molecular weight determination is of great significance, such as the determination of the first-level structure of the average protein, not only to determine the molecular weight of proteins, but also to determine the molecular weight of sub-base and oligomer and hydrolyzed, enzyme-based fragments of the molecular weight.
molecular weight determination mainly includes osmotic pressure method, light scattering method, super-speed high heart method, gel layering and polyacrylate amine gel electrophoresis. These methods have the disadvantages of high sample consumption and low accuracy, which are susceptible to the shape of proteins. . MALI-MS technology with its high sensitivity, accuracy has been widely used in the field of biomedical science, especially in protein analysis, has been analyzed hundreds of proteins, not only to determine a variety of hydrophobic, hydrophobic and glycoprotein molecular weight, but also directly used to determine the molecular weight of protein mixtures, can also be used to determine the degraded mixture such as enzymes to determine the amino acid sequence of peptides. This could be considered a major breakthrough in the field of protein analysis. Proteomics Proteomics Proteomics refers to all protein components expressed by a genome, cell, or tissue.
Proteomics study is to study the composition of proteins in cells or organisms and their activity patterns at the overall level, including the separation of all proteins in cells, the identification of protein expression patterns, protein identification, the analysis of protein translation modification and the construction of proteomic databases.
mass spectrometry technology, as one of the three supporting technologies for proteomics research, is widely used in peptide fingerprint spectrometry and amino acid sequence determination, in addition to the quality determination of peptides and proteins. PePtide Mass Fingerprinting (PMF) determination is a method of mass spectrometry of protease-degraded or degraded multi-peptide mixtures, comparing the peptides obtained from mass spectrometry with theoretical peptides of proteins in the peptide protein database to determine whether the protein being tested is known or unknown. Because different proteins have different amino acid sequences, the peptide tablets obtained by different proteins have the characteristics of fingerprints. the method of peptide fingerprinting has been studied on yeast, E. coli, heart muscle and other proteomics. The study of E. coli proteins transferred by PVDF membranes showed that three peptide tablets could achieve the correct identification of proteins.
results of yeast proteomics studies using in-place enzymatic methods show that about 90 percent of proteins are identified, and more than 30 new proteins have been found, which are open reading frameworks that are not recognized in yeast genome studies.
, the method of peptide fingerprinting is more reliable than amino acid composition analysis because MALDI measures peptide mass with 99. 9%, while the accuracy of amino acid composition analysis is only 90%. In addition, MALDI can withstand the presence of a small number of impurities, for the purity is not very high samples can also get the desired results. The determination of peptide sequence is often through series mass spectrometry technology to achieve the purpose of analysis, it uses different mass spectrometry technology to select ions with a specific mass-to-load ratio, and its collision induces high solution, by inferring the fracture of peptide tablets, the peptide sequence can be derived. Mass Spectrometry and Nucleic Acid Research Modern mass spectrometry technology has been very successful in the study of peptides and proteins since its inception, so people began to pay for the study of trait spectrometry technology for nucleic acids, in recent years, synthetic oligonucleotides and their analogotides as an antisophase in the treatment of viral infections and some cancers have good prospects, oligonucleotides as a drug its structural characteristics must be confirmed.
conventional chromatography or electrophoresis technology can only analyze its concentration and purity, but its base composition, sequence and other structural information can not be done. . The emergence of ESI and MALDI mass spectrometry technology provides a powerful method for the structural and sequence analysis of oligonucleotides and their analogi, which is the first partial degradation of oligonucleotide samples from the 3'' or 5' end with excision enzymes, and the sampling of mass spectrometry at different times. By comparing the molecular mass of two adjacent fragments, the molecular mass of the nucleotide monolith being cut can be calculated and compared with the standard molecular weight of the four deoxysides.
the problem of MALDI technology resolution makes it more suitable for the analysis of short-chain nucleic acids with less base reduction. How to obtain high-resolution DNA mass spectrometry has become a hot topic of research for a time, because the chemical structure of DNA has different structural characteristics from proteins, so that DNA samples have some particularities, one is the existence of phosphate groups in its structure, there is a tendency to form sodium phosphating ions; 1995, M. L. Vestal and others applied ion delay (lonDelayed Extraction, DE) technology to MALDI-MS, which not only improved the resolution of MALDI-MS, but also opened up a new field of mass spectrometrometromety in the field of DNA research. Domestic Deng Huimin and others also used DE-MALDI-MS method to determine the mixed base DNA, obtained a high-resolution DNA mass spectrometography. in addition to being used in protein and nucleic acid research, mass spectrometry and
clinical medicine mass spectrometry has been widely used in clinical medical testing with its sensitivity and high resolution, such as dynamic analysis of drug metabolites, identification of cancer cell proteins, detection of isotope markers, etc. Among them, 14C-Urea breath test with isotope 14C mark and 15N-labeled 15N-excretion test have become clinically detected gastric heliotrous screw.