Abstract: The present invention provides a method for effectively introducing sulfonic acid groups into the N-terminus of a protein or a peptide. The method comprises a modification step to react a N-terminus in a protein or peptide with a compound A which includes disulfide group and a cleavage step to cleave a disulfide bond of the disulfide group to convert into a sulfonic acid group. The present invention also provides a method of analyzing proteins or peptides easily and effectively on mass spectrometry and an intermediate that can be used to effectively derivatize proteins or peptides as sulfonic acid derivatives.

Abstract: A method of mass-producing minute structures such as biochips, protein chips, quantum dots, and quantum chips involves arranging an antigen two-dimensionally on a board and arranging probes two-dimensionally facing the same direction so that the binding sites of the probes may bind to the antigen. An inorganic substance such as Ni is deposited on the board from the upper side of the probes by sputtering or evaporation to form a thin film layer and on the top surface of the flatly formed thin film layer, a supporting layer is formed by separating out the same inorganic substance using electrotyping. Then, by peeling the thin film layer and the supporting layer off of the board together, the mother stamper having cavities for the patterns of biomolecules is obtained.

Abstract: At both ends of a waveguide 43 having a plurality of cores 51, light emitting elements 47 and light receiving elements 49 are disposed so as to face end faces of the cores 51. A switch 44 is overlapped over the waveguide 43. In the switch 44, switching windows 52 each can be switched between a state where light propagating through the core 51 is passed and a state where the light is reflected are arranged in the vertical and horizontal directions, and the switching windows 52 are arranged along the top faces of the cores 51. A test board 45 having a plurality of channels 60 in each of which a metallic thin film 61 is formed is disposed over the switch 44, and receptors 62 are fixed on the metallic thin film 61 in the channels 60. A specimen containing a specific ligand is passed in each of the channels 60.

Abstract: In a surface plasmon resonance sensor including a chip with a substrate 102 and a metal layer 103, a prism 104, an optical system 105 serving as a light source, and a light detector 106, the metal layer 103 is configured by a flat part 109 formed into a thin film, and convex parts formed from metal particles 110 and the like arranged spaced apart from each other. When light enters the metal layer 103 of such configuration, resonance angle arising from the flat part 109 and the convex parts are respectively obtained. The change in index of refraction of a medium contacted by the metal layer is detected from such resonance angle.

Abstract: A simple and low-cost method of selectively modifying the C-terminal of a protein or peptide is provided. A method of modifying the C-terminal of a protein or peptide comprises forming an intramolecular oxazolone ring at the C-terminal of the protein or peptide that requires C-terminal modification, and then performing a ring-opening of the oxazolone ring to produce a protein or peptide with a modified C-terminal.

Abstract: At both ends of a waveguide 43 having a plurality of cores 51, light emitting elements 47 and light receiving elements 49 are disposed so as to face end faces of the cores 51. A switch 44 is overlapped over the waveguide 43. In the switch 44, switching windows 52 each can be switched between a state where light propagating through the core 51 is passed and a state where the light is reflected are arranged in the vertical and horizontal directions, and the switching windows 52 are arranged along the top faces of the cores 51. A test board 45 having a plurality of channels 60 in each of which a metallic thin film 61 is formed is disposed over the switch 44, and receptors 62 are fixed on the metallic thin film 61 in the channels 60. A specimen containing a specific ligand is passed in each of the channels 60.

Abstract: The present invention provides a method for selectively collecting the N-terminal peptide fragments of a protein of interest whether or not the protein of interest is modified on the N-terminus.

Abstract: A simple and low-cost method of selectively modifying the C-terminal of a protein or peptide is provided. A method of modifying the C-terminal of a protein or peptide comprises forming an intramolecular oxazolone ring at the C-terminal of the protein or peptide that requires C-terminal modification, and then performing a ring-opening of the oxazolone ring to produce a protein or peptide with a modified C-terminal.

Abstract: The present invention provides a method for effectively introducing sulfonic acid groups into the N-terminus of a protein or a peptide; a method capable of analyzing proteins or peptides easily and effectively on mass spectrometry; an intermediate that can be used to effectively derivatize proteins or peptides as sulfonic acid derivatives. A method for derivatizing a protein or peptide to a sulfonic acid derivative, comprising steps of: modification step to react a N-terminus in a protein or peptide with a compound A which includes disulfide group, to obtain a protein or peptide modified with the compound A at the N-terminus; and cleavage step to cleave a disulfide bond of the disulfide group to convert into a sulfonic acid group, thereby converting the modified protein or peptide into a sulfonic acid derivative. A method for analyzing the amino acid sequence of a protein or peptide, wherein the sulfonic acid derivative of a protein or a peptide obtained by the above method is subjected to mass spectrometry.

Abstract: A method of mass-producing minute structures such as biochips, protein chips, quantum dots, and quantum chips involves arranging an antigen two-dimensionally on a board and arranging probes two-dimensionally facing the same direction so that the binding sites of the probes may bind to the antigen. An inorganic substance such as Ni is deposited on the board from the upper side of the probes by sputtering or evaporation to form a thin film layer and on the top surface of the flatly formed thin film layer, a supporting layer is formed by separating out the same inorganic substance using electrotyping. Then, by peeling the thin film layer and the supporting layer off of the board together, the mother stamper having cavities for the patterns of biomolecules is obtained.

Abstract: The present invention provides a method for determining amino acid sequences of peptides involving the use of a mass spectrometer that not only offers a high decomposition efficiency into fragment ions and a high selectivity of cleavage sites for a wide variety of peptide including peptides of unknown identity, but also achieves highly sensitive, high-throughput detection of the resulting fragment ions. A method for determining amino acid sequence of a peptide, comprising the steps of: preparing a peptide of interest or fragments thereof obtained by optionally cleaving the peptide of interest; coupling an amino acid derivative to the N-terminus of the peptide of interest or the fragments thereof, the amino acid derivative having protected an amino group with a protective group and derived from an amino acid with a side chain containing an acidic group; and subjecting the coupled product to mass spectrometry analysis.

Abstract: The present invention provides a method for selectively collecting the N-terminal peptide fragments of a protein of interest whether or not the protein of interest is modified on the N-terminus.

Abstract: The present invention provides a novel metal complex useful for a reagent for determining the amino acid sequence of protein or peptide, and a method of using it for determining the amino acid sequence of protein or peptide. The metal complex which has a functional group capable of forming a covalent bond with the amino group of the N-terminal amino acid residue of protein or peptide or with the carboxyl group of the C-terminal amino acid residue of protein or peptide. In general, the functional group is in the ligand of the complex.