Abstract: A method for isolating proteins from prokaryotes is disclose. The method enables easy break down of bacterial cell walls to obtain intact proteins without damage by a simple process of adding organic solvents including lower alcohols or nitrile derivatives; or applying osmotic stimulation to samples containing pathogenic bacteria or the like. The method may be usefully applied to rapid and accurate identification of periplasmic proteins of gram-negative bacteria without additional purification process.

Abstract: The present invention relates to a method for detecting a pathogenic strain having resistance to carbapenem antibiotics in a biological sample. According to the present invention, it is possible to directly identify carbapenemases, specifically KPC, OXA, NDM, IMP, VIM and/or GES protein, by mass spectrometry, thereby making it possible to quickly determine not only whether a pathogenic strain has resistance to antibiotics, but also the type of protein involved in the resistance. According to the present invention, the physical and chemical properties of each carbapenemase in vivo, such as the unique N-terminal truncation length, methionine residue oxidation and disulfide bond formation in each type of carbapenemase, are identified and are reflected on reference mass values.

Abstract: The present invention relates to a method for detecting a pathogenic strain having resistance to ?-lactam antibiotics in a biological sample, and a method for identifying a protein involved in resistance in ?-lactam antibiotics, which is contained in a biological sample. According to the present invention, it is possible to quickly and accurately determine not only whether a pathogenic strain has resistance to antibiotics, but also the type of protein involved in the resistance, by directly identifying an extended spectrum ?-lactamase (ESBL) protein with a truncated N-terminus through mass spectrometry. Accordingly, the present invention can be effectively utilized to quickly establish an appropriate antibiotic administration strategy at the initial stage of infection.

Abstract: This invention relates to a photocleavable mass tag and the use thereof, and particularly to a thiochromene-type compound useful for MALDI-TOF (Matrix-Assisted Laser Desorption/Ionization Time-Of-Flight) mass spectrometry or matrix-less LDI-TOF (Laser Desorption/Ionization Time-Of-Flight) mass spectrometry and the use thereof.

Abstract: This invention relates to a photocleavable mass tag and the use thereof, and particularly to a thiochromene-type compound useful for MALDI-TOF (Matrix-Assisted Laser Desorption/Ionization Time-Of-Flight) mass spectrometry or matrix-less LDI-TOF (Laser Desorption/Ionization Time-Of-Flight) mass spectrometry and the use thereof.

Abstract: The present invention relates to a thermostable alpha-1-antitrypsin mutein with a disulfide bond and a preparation method of the same, more precisely an alpha-1-antitrypsin mutein with improved thermostability, compared with the conventional thermostable alpha-1-antitrypsin mutein (Korean Patent No. 133252), resulted from the process of substituting the 168th and 189th amino acids of the alpha-1-antitrypsin with cysteines which are then linked by a disulfide bond, with keeping its alpha-1-antitrypsin activity unchanged, and a preparing method of the same. The thermostable alpha-1-antitrypsin mutein with a disulfide bond of the invention can be effectively used for a protein based therapeutic agent which is very stable in vivo, and can be applied further in various fields including in the development of a diagnostic reagent and in the preparation of an affinity column.

Abstract: The present invention relates to a thermostable alpha-1-antitrypsin mutein with a disulfide bond and a preparation method of the same, more precisely an alpha-1-antitrypsin mutein with improved thermostability, compared with the conventional thermostable alpha-1-antitrypsin mutein (Korean Patent No. 133252), resulted from the process of substituting the 168th and 189th amino acids of the alpha-1-antitrypsin with cysteines which are then linked by a disulfide bond, with keeping its alpha-1-antitrypsin activity unchanged, and a preparing method of the same. The thermostable alpha-1-antitrypsin mutein with a disulfide bond of the invention can be effectively used for a protein based therapeutic agent which is very stable in vivo, and can be applied further in various fields including in the development of a diagnostic reagent and in the preparation of an affinity column.