Abstract: 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.

Abstract: A multiplex proteome quantification method based on isobaric dimethyl labeling implements dimethyl labeling of peptide N-terminal in an acidic condition and C-terminal in an alkaline condition one after another by means of Hall the property that a dimethylation reaction has different rates on an amino group at the peptide N-terminal and an amino group on a Lysine side chain at the peptide C-terminal in the acidic condition. Multiplex labeling of peptide samples is implemented by means of the organic combination of various isotope forms of a dimethyl labeling reagents. The mass-to-charge ratios in MS1 of peptides after multiplex labeling are completely the same, the mass-to-charge ratios of the fragment ions in MS2 are different, and multiplex quantitative analyses are carried out by extracting the intensity values of corresponding fragment ions in the MS2.

Abstract: 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.

Abstract: An integrated system has functions of high-abundance protein depletion, on-line denaturation and reduction of middle and low-abundance proteins, desalting and protein digestion. This system includes an antibody column for the depletion of high-abundance protein from body fluids, clustering hollow fiber membranes based high temperature denaturator and reducer, solvent exchanger and immobilized enzymatic reactor. The protein sample from body fluid is firstly treated by antibody column to remove the high-abundance proteins, and then the eluted medium-low abundance protein is subjected to on-line, rapid denaturation and reduction by a high-temperature denaturator and reducer, subsequently the denaturing and the reducing agents in proteins are removed by a solvent exchanger, finally the purified proteins were enzymatically hydrolyzed by an immobilized enzymatic reactor. The peptides produced by the enzymatic hydrolysis can be analyzed by mass spectrometry (MS).

Abstract: A multiplex proteome quantification method based on isobaric dimethyl labeling, which implements dimethyl labeling of peptide N-terminal in an acidic condition and C-terminal in an alkaline condition one after another by means of a property that a dimethylation reaction has different rates on an amino group at the peptide N-terminal and an amino group on a Lysine side chain at the peptide C-terminal in the acidic condition. Multiplex labeling of peptide samples is implemented by means of the organic combination of various isotope forms of a dimethyl labeling reagents. The mass-to-charge ratios in MS1 of peptides after multiplex labeling are completely the same, the mass-to-charge ratios of the fragment ions in MS2 are different, and multiplex quantitative analyses are carried out by extracting the intensity values of corresponding fragment ions in the MS2.

Abstract: The present invention relates to a biphasic microreactor for membrane proteins pretreatment comprising cation exchange and anion exchange materials packed in sequence in a container as stationary phase, where membrane proteins capture, pH adjustment, reduction, alkylation and tryptic digestion processed in situ. Thus the microreactor has advantages of high recovery, ease of operation, high efficiency and high throughput.

Abstract: A call processing method, service control device and call processing system is provided. The method includes: correspondence relationship between a called number and a manage number is pre-established; service authentication of a caller is performed upon reception of information on a call request initiated by the caller to the called number; a call to the called number is initiated with the management number after authentication is passed; and a called terminal identifies the managed number and sets up communication with the caller after identification is passed, thereby avoiding direct calling of the caller to the called number without any authentication flow and improving service security.