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: A method of evaluating a cell state based on information of an image taken of a cell containing a chromosome territory is provided. This method includes extracting the chromosome territory from the image (S20), standardizing a positioning state of the chromosome territory and then quantifying the positioning state (S22), and evaluating the cell state based on the quantified positioning state of the chromosome territory (S26).

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: 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 method of evaluating a cell state based on information of an image taken of a cell containing a chromosome territory is provided. This method includes extracting the chromosome territory from the image (S20), standardizing a positioning state of the chromosome territory and then quantifying the positioning state (S22), and evaluating the cell state based on the quantified positioning state of the chromosome territory (S26).

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