Abstract: The present invention provides a method for analyzing the C-terminal amino acid sequence of a peptide by using a reaction for successively releasing the C-terminal amino acids of the peptide, which method can suppress, when successively releasing the C-terminal amino acids of a peptide of long amino acid length, such a undesirable side reaction as cleavage of peptide bond in the intermediate position of the peptide and can carry out the chemical treatment thereof under widely applicable conditions; In the method, a dry sample of a peptide with long amino acid length is beforehand subjected to an N-acylation treatment; by using a reaction reagent where an alkanoic acid anhydride is combined with a small amount of a perfluoroalkanoic acid, successive release of C-terminal amino acids is conducted under mild conditions; a hydrolysis treatment is applied; then, selective fragmentization at site of arginine residue is performed by digestion by trypsin; thereafter, decreases in molecular weight are measured for the

Abstract: The present invention provides a method for analyzing the C-terminal amino acid sequence of a peptide by using a reaction for successively releasing the C-terminal amino acids of the peptide, which method can suppress, when successively releasing the C-terminal amino acids of a peptide of long amino acid length, such a undesirable side reaction as cleavage of peptide bond in the intermediate position of the peptide and can carry out the chemical treatment thereof under widely applicable conditions; In the method, a dry sample of a peptide with long amino acid length is beforehand subjected to an N-acylation treatment; by using a reaction reagent where an alkanoic acid anhydride is combined with a small amount of a perfluoroalkanoic acid, successive release of C-terminal amino acids is conducted under mild conditions; a hydrolysis treatment is applied; then, selective fragmentization at site of arginine residue is performed by digestion by trypsin; thereafter, decreases in molecular weight are measured for the

Abstract: The present invention provides a method for analyzing the C-terminal amino acid sequence of a peptide by using a reaction for successively releasing the C-terminal amino acids of the peptide, which method can suppress, when successively releasing the C-terminal amino acids of a peptide of long amino acid length, such a undesirable side reaction as cleavage of peptide bond in the intermediate position of the peptide and can carry out the chemical treatment thereof under widely applicable conditions; In the method, a dry sample of a peptide with long amino acid length is beforehand subjected to an N-acylation treatment; by using a reaction reagent where an alkanoic acid anhydride is combined with a small amount of a perfluoroalkanoic acid, successive release of C-terminal amino acids is conducted under mild conditions; a hydrolysis treatment is applied; then, selective fragmentization at site of arginine residue is performed by digestion by trypsin; thereafter, decreases in molecular weight are measured for the

Abstract: Provided are: a method of assessing hepatocellular carcinoma by using a protein with a different phosphorylated state in hepatocellular carcinoma cells compared with non-hepatocellular carcinoma cells; and a hepatocellular carcinoma protein marker for detecting hepatocellular carcinoma formed of the protein. The hepatocellular carcinoma protein marker for detecting hepatocellular carcinoma includes tumor rejection antigen gp96 formed of the amino acid represented by SEQ ID NO: 1, and is measured for its phosphorylated state to detect the presence or absence of hepatocellular carcinoma.

Abstract: A pathological diagnosis support device, a pathological diagnosis support program, a pathological diagnosis support method, and a pathological diagnosis support system extract a pathological tissue for diagnosis from a pathological image and diagnose the pathological tissue. A tissue collected in a pathological inspection is stained using, for example, hematoxylin and eosin. In consideration of the state of the tissue in which a cell nucleus and its peripheral constituent items are stained in respective colors unique thereto, subimages such as a cell nucleus, a pore, cytoplasm, interstitium are extracted from the pathological image, and color information of the cell nucleus is also extracted. The subimages and the color information are stored as feature candidates so that presence or absence of a tumor and benignity or malignity of the tumor are determined.

Abstract: Whether a patient actually takes medicine or not is traced and recorded. The used state of a packaged object is traced and recorded. Specifically, a passive wireless tag and an antenna are attached to a packaged object management device. The passive wireless tag is disposed on the package containing a packaged object, and power is generated in the passive wireless tag by electromagnetic induction (contactless power transmission) through a radio wave from a reader, and the passive wireless tag receives/transmits a radio wave to transmit/receive information. The antenna is disposed in a region (take-out opening) for taking out the packaged object from the package so that the antenna can be broken when the packaged object is taken out and is used to inform the passive wireless tag of the take-out of the packaged object. The gap between the boundary of the region (take-out opening) for taking out the packaged object and the antenna is smaller than the minimum width large enough to take out the packaged object.

Abstract: The present invention provides, as a method of analyzing the C-terminal amino acid sequence of a peptide with use of reaction technique for successively releasing the C-terminal amino acids, in which undesirable side reactions, such as cleavage of a peptide bond at the middle of the peptide, can be prevented and chemical treatments therein can be carried out under widely applicable conditions in the course of successive release of the C-terminal amino acids from a peptide, such a method comprising steps of dehydrating the gel on which a target peptide that has been separated by gel electrophoresis is held in the bound state; immersing it in a mixture solution of an alkanoic acid anhydride added with a small amount of a perfluoroalkanoic acid in a dipolar aprotic solvent to re-swell the gel carrier, forming a 5-oxazolone structure, at a temperature chosen in the range of from 30° C. to 80° C.

Abstract: After anonymization of individual information such as clinical data, only the owner of a specimen data or the owner of a browsing right can identify data stored or related to it after the anonymization. Therefore, in an unlinkable anonymizing method, a uni-directional function such as a hash value calculation is applied to a combination data of related information such as an individual identifiable ID number or data, ID information and a key symbol in case of the anonymization, or a relational data such as a specimen number from only which an individual cannot be identified. A correspondence table of the anonymization number and the individual information is deleted. An estimation of an original individual or a specimen number from the anonymization number is prevented by use of uni-directional function. The access to the data after the anonymization is limited only to the owner who knows anonymization key data or the mandatory of the information.

Abstract: The present invention provides, as for a method for analyzing the C-terminal amino acid sequence of a peptide by using a reaction for successively releasing the C-terminal amino acids of the peptide, which method can suppress, when successively releasing the C-terminal amino acids of a peptide of long amino acid length, such a undesirable side reaction as cleavage of peptide bond in the intermediate position of the peptide and can carry out the chemical treatment thereof under widely applicable conditions, a following method wherein a dry sample of a peptide with long amino acid length is beforehand subjected to an N-acylation treatment; by using a reaction reagent where an alkanoic acid anhydride is combined with a small amount of a perfluoroalkanoic acid, successive release of C-terminal amino acids is conducted under mild conditions; a hydrolysis treatment is applied; then, selective fragmentization at site of arginine residue is performed by digestion by trypsin; thereafter, decreases in molecular weight

Abstract: A protein search method for searching for, as a target protein, a protein having direct or indirect relevance to information based on protein representation profiling data acquired by means of proteome analysis includes: determining, as a target protein, a protein that is relevant to the information based on significance of proteins obtained by using supervised learning from the information and the protein representation in the profiling data; and evaluating the performance of the target protein by means of evaluation data.

Abstract: An analyte peptide is selectively degraded sequentially by using an alkanoic anhydride (S101). The original peptide and a series of degradation reaction products having peptide in which one or more C-terminal-sided amino acids are deleted, are subjected to a certain posttreatment (S102). The molecular weight of the reaction products is measured by mass spectrometry (S103). And, the amino acid sequence of the original peptide from C-terminal is determined, based on the molecular weight obtained by mass spectrometry (S104).

Abstract: The primary structure or the modification state of a protein is analyzed in detail. First, an analyte protein is subjected to PMF analysis (S101), and the gene of the protein is identified. Unidentified peaks not corresponding to the peaks of hypothetical peptide fragments are extracted, by comparing the hypothetical mass spectrum with the mass spectrum obtained by mass spectrometry of a sample protein (S102). Then, the unidentified peaks obtained are analyzed, and thus, the structure or properties of the protein, the presence and the kind of modification of amino acid residues, amino acid substitution, generation of mutants, and terminal cleavage are analyzed (S103).

Abstract: An analyte peptide is selectively degraded sequentially by using an alkanoic anhydride (S101). The original peptide and a series of degradation reaction products having peptide in which one or more C-terminal-sided amino acids are deleted, are subjected to a certain posttreatment (S102). The molecular weight of the reaction products is measured by mass spectrometry (S103). And, the amino acid sequence of the original peptide from C-terminal is determined, based on the molecular weight obtained by mass spectrometry (S104).

Abstract: The present invention provides a method for analyzing the C-terminal amino acid sequence of a peptide by applying reaction technique for successively releasing the C-terminal amino acids therefrom, which method can suppress, when releasing the C-terminal amino acids of the peptide in sequence, such as an undesirable side reaction as cleavage of peptide bond in the intermediate position of the peptide, and allows to carry out the chemical treatment thereof under widely applicable conditions. In the method according to the present invention, an alkanoic acid anhydride and a perfluoroalkanoic acid both of vapor phase, which are supplied from a mixture containing an alkanoic acid anhydride with a small amount of a perfluoroalkanoic acid added thereto, are allowed to act on a dry sample of the peptide to be examined in a dry atmosphere at a temperature chosen in a range of 15 to 60° C.

Abstract: The present invention provides an approach for identifying with high accuracy, a known protein or a variant of the known protein derived from the same genomic gene as in a target protein to be analyzed, based on a mass spectrometric result of a plurality of peptide fragments obtained from site-specific enzymatic digestion of the target protein to be analyzed by referring to nucleotide sequences of genes encoding known proteins on a database and to deduced full-length amino acid sequences thereof.

Abstract: A biomolecule is analyzed with high accuracy. A biomolecule is analyzed with high likelihood. A biomolecule as an analysis subject is modified with a marker binding or adsorbing to only its specific portion (S101). Next, the biomolecule modified with the marker is developed on a base plate (S102). The arrangement of the biomolecule on the base plate is detected using a marker (S103). Then, scanning is performed along the shape of the biomolecule present on the detected position (S104). The biomolecule is analyzed based on an information relating to the shape or arrangement of the biomolecule obtained by scanning or an information relating to the arrangement of the marker on the biomolecule (S105).

Abstract: In order to generate a risk index of stress symptoms triggered by flashing lights on a scan type video display screen, a video signal processor is provided which operates such as to implement temporal filtering and spatial filtering on a video signal applied thereto every field and detect low temporal frequency components while excluding effects due to high spatial frequencies. A risk index generator receives the low frequency components from the video signal processor and determines the risk index based thereon.

Abstract: Provided a method of acquiring information on internal sequence which is applicable to a trace amount of protein and has a high reliability. A protein to be analyzed is limitedly cleaved at a specified position of amino acid to prepare a mixture of a plurality of peptide fragments; one or more peptide fragments are isolated and purified from the peptide fragment mixture; C-terminal amino acids of the isolated and purified peptide fragment are successively released by chemical reaction to prepare a mixture containing a series of resulting products; mass spectrometry is applied to both the reaction products of the successive truncation and unreacted peptide fragment not subjected to the successive truncation reaction; then results of the mass spectrometry is analyzed to acquire chemical structure information of the target protein.

Abstract: The present invention provides a method for analyzing the C-terminal amino acid sequence of a peptide by using a reaction for successively releasing the C-terminal amino acids of the peptide, which method can suppress, when successively releasing the C-terminal amino acids of a peptide of long amino acid length, such a undesirable side reaction as cleavage of peptide bond in the intermediate position of the peptide and can carry out the chemical treatment thereof under widely applicable conditions; In the method, a dry sample of a peptide with long amino acid length is beforehand subjected to an N-acylation treatment; by using a reaction reagent where an alkanoic acid anhydride is combined with a small amount of a perfluoroalkanoic acid, successive release of C-terminal amino acids is conducted under mild conditions; a hydrolysis treatment is applied; then, selective fragmentization at site of arginine residue is performed by digestion by trypsin; thereafter, decreases in molecular weight are measured for the

Abstract: A pathological diagnosis support device, a pathological diagnosis support program, a pathological diagnosis support method, and a pathological diagnosis support system extract a pathological tissue for diagnosis from a pathological image and diagnose the pathological tissue. A tissue collected in a pathological inspection is stained using, for example, hematoxylin and eosin. In consideration of the state of the tissue in which a cell nucleus and its peripheral constituent items are stained in respective colors unique thereto, subimages such as a cell nucleus, a pore, cytoplasm, interstitium are extracted from the pathological image, and color information of the cell nucleus is also extracted. The subimages and the color information are stored as feature candidates so that presence or absence of a tumor and benignity or malignity of the tumor are determined.