Abstract: Abstract The disclosure provides a reagent comprising a leuco dye and a compound represented by Formula (I): where R represents a hydrocarbon chain having 8 to 17 carbon atoms, the reagent for measuring glycoprotein, a kit comprising the reagent and a second reagent, and methods of measuring hemoglobin A1c using the reagent.

Abstract: Provided is a method for measuring a glycoprotein using an enzymatic method, and the method includes simplified steps.

Abstract: Provided is a reagent that is suitable for measurement of a glycoprotein and contains a compound capable of stabilizing a leuco dye.

Abstract: Provided is a method for measuring a glycoprotein using an enzymatic method, and the method includes simplified steps.

Abstract: A communication control apparatus includes a communication control unit executing a requested communication service via a wireless unit selected from a plurality of wireless units. The communication services are assigned with different priorities; the wireless units are assigned with different priorities. Suppose that a communication service, which is newly requested, has a priority higher than that on a communication service that is being executed. The communication control unit executes the newly requested communication service via a wireless unit having the highest priority among all of usable wireless units.

Abstract: An electrophoresis chip that can be small and simple and that can analyze a sample with high accuracy is provided. The electrophoresis chip includes an upper substrate 4, a lower substrate 1, an introduction reservoir 2a, a recovery reservoir 2b and a capillary channel for sample analysis 3x. The introduction reservoir 2a and the recovery reservoir 2b are formed in the lower substrate 1. The introduction reservoir 2a and the recovery reservoir 2b are in communication with each other via the capillary channel for sample analysis 3x. The introduction reservoir 2a receives a sample to be measured. The sample is electrophoretically introduced directly into the capillary channel for sample analysis 3x by creating a potential difference between the introduction reservoir 2a and the recovery reservoir 2b, and is also analyzed in the capillary channel for sample analysis 3x during the separation of the sample while the sample is being continuously supplied.

Abstract: A communication control apparatus includes a communication control unit executing a requested communication service via a wireless unit selected from a plurality of wireless units. The communication services are assigned with different priorities; the wireless units are assigned with different priorities. Suppose that a communication service, which is newly requested, has a priority higher than that on a communication service that is being executed. The communication control unit executes the newly requested communication service via a wireless unit having the highest priority among all of usable wireless units.

Abstract: A process for analyzing a sample by a capillary electrophoresis method is provided that allows for high analytic precision and reduction in apparatus size, and can be readily carried out by electrophoresing a complex of a sample and an anionic group-containing compound in the capillary channel, wherein the capillary channel includes an A layer that is coated on an inner wall thereof and a B layer that is coated on the A layer, where the A and B layers are as described.

Abstract: A process for analyzing a sample by a capillary electrophoresis method is provided that allows for high analytic precision and reduction in apparatus size, and can be readily carried out by electrophoresing a complex of a sample and an anionic group-containing compound in the capillary channel, wherein the capillary channel includes an A layer that is coated on an inner wall thereof and a B layer that is coated on the A layer, where the A and B layers are as described.

Abstract: The present invention provides a device that decreases deformation during manufacturing of the device, provides a firm joint without use of an adhesive, and allows chemical modification of a channel during manufacturing of the device. The device includes two joined substrates, and a concavity is formed on at least one of the opposing surfaces of the two substrates so as to make a channel, where the two substrates are joined together by a covalent bond via a crosslinking agent (A), and the crosslinking agent (A) is exposed on an inner wall surface of the channel.

Abstract: A method for measuring an analyte is described that includes the steps of: i) preparing a reagent (D) in which an enzyme (A) and an enzyme (B) coexist in the absence of the analyte; ii) bringing the analyte into contact with the enzyme (A) and the enzyme (B) so that the enzyme (A) acts on the analyte to produce a product (E), on which the enzyme (B) does not substantially act, from the analyte; iii) producing a product (C) by allowing the enzyme (A) or an enzyme (F) that is different from the enzyme (A) that acts on the analyte to produce a product (C) to act on the analyte and/or the product (E); and iv) detecting the product (C) by the enzyme (B).

Abstract: An analysis apparatus is provided with a storage tank, an injection nozzle, a syringe, a collection nozzle, a test sample tank, a microchip having two or more separation channels, detectors, a waste liquid tank, a controller, and a power supply. The collection nozzle collects a specimen which becomes a test sample from a test sample container housing the specimen, and transfers the specimen to the test sample tank. The separation channels separate characteristic components contained in the test sample. The injection nozzle is distanced from the collection nozzle and injects the test sample from the test sample tank into the separation channels. The detectors detect the separated characteristic components in the separation channels.

Abstract: The present invention provides a stabilizer that can stabilize a salt of 10-(carboxymethylaminocarbonyl)-3,7-bis(dimethylamino)phenothiazine or a derivative thereof even under the existence of moisture or under light irradiation. A compound described in at least one of (1) and (2) below is used as the stabilizer of the salt of 10-(carboxymethylaminocarbonyl)-3,7-bis(dimethylamino)phenothiazine or the derivative thereof.

Abstract: A method for analyzing hemoglobin by electrophoresis, capable of analyzing hemoglobin A1c (HbA1c) and modified hemoglobin with improved accuracy in a shortened analysis time is provided. The method for analyzing hemoglobin by electrophoresis includes performing electrophoresis under conditions in which an acidic substance having two or more carboxyl groups is present in an electrophoresis solution. At least two of the carboxyl groups of the acidic substance each have an acid dissociation constant (pKa) lower than the pH of the electrophoresis solution at the time of analysis.

Abstract: The present invention provides a method of pretreating a sample containing a glycated amine as an analyte, thereby enabling highly reliable measurement of a glycated amine. A glycated amino acid in the sample is degraded by causing a fructosyl amino acid oxidase (FAOD) to act thereon, and thereafter, a FAOD further is caused to act on the glycated amine as the analyte in the sample to cause a redox reaction. The amount of the glycated amine is determined by measuring the redox reaction. The substrate specificity of the FAOD caused to act on the glycated amino acid may be either the same as or different from that of the FAOD caused to act on the glycated amine. When using the same FAOD, a FAOD is caused to act on the glycated amino acid to degrade it, and thereafter, the sample is treated with a protease to inactivate the FAOD and also to degrade the glycated amine.

Abstract: The present invention provides a method of pretreating a sample containing a glycated amine as an analyte, thereby enabling highly reliable measurement of a glycated amine. A glycated amino acid in the sample is degraded by causing a fructosyl amino acid oxidase (FAOD) to act thereon, and thereafter, a FAOD further is caused to act on the glycated amine as the analyte in the sample to cause a redox reaction. The amount of the glycated amine is determined by measuring the redox reaction. The substrate specificity of the FAOD caused to act on the glycated amino acid may be either the same as or different from that of the FAOD caused to act on the glycated amine. When using the same FAOD, a FAOD is caused to act on the glycated amino acid to degrade it, and thereafter, the sample is treated with a protease to inactivate the FAOD and also to degrade the glycated amine.

Abstract: The present invention provides a method of pretreating a sample containing a glycated amine as an analyte, thereby enabling highly reliable measurement of a glycated amine. A glycated amino acid in the sample is degraded by causing a fructosyl amino acid oxidase (FAOD) to act thereon, and thereafter, a FAOD further is caused to act on the glycated amine as the analyte in the sample to cause a redox reaction. The amount of the glycated amine is determined by measuring the redox reaction. The substrate specificity of the FAOD caused to act on the glycated amino acid may be either the same as or different from that of the FAOD caused to act on the glycated amine. When using the same FAOD, a FAOD is caused to act on the glycated amino acid to degrade it, and thereafter, the sample is treated with a protease to inactivate the FAOD and also to degrade the glycated amine.

Abstract: A method of determining glycated hemoglobin is provided, by which a ratio of the glycated hemoglobin in a sample can be determined accurately and easily. The ratio of glycated hemoglobin can be determined by degrading a glycated hemoglobin in a whole blood sample selectively with a protease to give a glycated hemoglobin degradation product; causing a redox reaction between a glycation site of the glycated hemoglobin degradation product and a fructosyl amino acid oxidoreductase; and determining this redox reaction. Further, as shown in FIG. 1, in a whole blood sample, there is a correlation between the ratio of the glycated hemoglobin determined by this method and an HbA1c concentration. Thus, without determining the glycated ?-amino group as a characteristic structure of HbA1c, an amount of HbA1c can be determined accurately and easily from the determined ratio of the glycated hemoglobin.

Abstract: A method of determining glycated hemoglobin is provided, by which a ratio of the glycated hemoglobin in a sample can be determined accurately and easily. The ratio of glycated hemoglobin can be determined by degrading a glycated hemoglobin in a whole blood sample selectively with a protease to give a glycated hemoglobin degradation product; causing a redox reaction between a glycation site of the glycated hemoglobin degradation product and a fructosyl amino acid oxidoreductase; and determining this redox reaction. Further, as shown in FIG. 1, in a whole blood sample, there is a correlation between the ratio of the glycated hemoglobin determined by this method and an HbA1c concentration. Thus, without determining the glycated ?-amino group as a characteristic structure of HbA1c, an amount of Hba1c can be determined accurately and easily from the determined ratio of the glycated hemoglobin.

Abstract: A method of determining glycated hemoglobin is provided, by which a ratio of the glycated hemoglobin in a sample can be determined accurately and easily. The ratio of glycated hemoglobin can be determined by degrading a glycated hemoglobin in a whole blood sample selectively with a protease to give a glycated hemoglobin degradation product; causing a redox reaction between a glycation site of the glycated hemoglobin degradation product and a fructosyl amino acid oxidoreductase; and determining this redox reaction. Further, as shown in FIG. 1, in a whole blood sample, there is a correlation between the ratio of the glycated hemoglobin determined by this method and an HbA1c concentration. Thus, without determining the glycated ?-amino group as a characteristic structure of HbA1c, an amount of HbA1c can be determined accurately and easily from the determined ratio of the glycated hemoglobin.