Disclosed are methods and kits for analyzing a sample comprising 1,5-anhydroglucitol and a possible first analyte via one or more chemiluminescent reactions. Certain embodiments include measuring a first light response resulting from a first chemiluminescent reaction and measuring a second light response resulting from a second chemiluminescent reaction. Certain embodiments also include comparing the first light response to the second light response to determine a ratio of 1,5-anhydroglucitol and the first analyte. Also provided are kits including reagents for practicing the claimed methods.

The present invention provides a measuring method for at least one of a kinase forward reaction substrate, a phosphorylated product thereof, and a precursor thereof, and includes a step of conducting an enzymatic cycling reaction by bringing at least a kinase, a first nucleotide coenzyme of the kinase, and a second nucleotide coenzyme having a different nucleoside moiety from the first nucleotide coenzyme into contact with a sample; a step of detecting a signal corresponding to a change of at least one of the first nucleotide coenzyme and a conversion product thereof, and the second nucleotide coenzyme and a conversion product thereof; and (3) a step of calculating, on the basis of the detected change of the signal, an amount of the kinase forward reaction substrate and/or the phosphorylated product thereof contained in the sample.

The present invention provides a measuring method for at least one of a kinase forward reaction substrate, a phosphorylated product thereof, and a precursor thereof, and includes a step of conducting an enzymatic cycling reaction by bringing at least a kinase, a first nucleotide coenzyme of the kinase, and a second nucleotide coenzyme having a different nucleoside moiety from the first nucleotide coenzyme into contact with a sample; a step of detecting a signal corresponding to a change of at least one of the first nucleotide coenzyme and a conversion product thereof, and the second nucleotide coenzyme and a conversion product thereof; and (3) a step of calculating, on the basis of the detected change of the signal, an amount of the kinase forward reaction substrate and/or the phosphorylated product thereof contained in the sample.

Devices and methods that can detect and control an individual polymer in a mixture is acted upon by another compound, for example, an enzyme, in a nanopore are provided. The devices and methods also determine (˜>50 Hz) the nucleotide base sequence of a polynucleotide under feedback control or using signals generated by the interactions between the polynucleotide and the nanopore. The invention is of particular use in the fields of molecular biology, structural biology, cell biology, molecular switches, molecular circuits, and molecular computational devices, and the manufacture thereof.

Devices and methods that can detect and control an individual polymer in a mixture is acted upon by another compound, for example, an enzyme, in a nanopore are provided. The devices and methods also determine (˜>50 Hz) the nucleotide base sequence of a polynucleotide under feedback control or using signals generated by the interactions between the polynucleotide and the nanopore. The invention is of particular use in the fields of molecular biology, structural biology, cell biology, molecular switches, molecular circuits, and molecular computational devices, and the manufacture thereof.

The present invention provides a novel glucose dehydrogenase that has excellent substrate specificity and that is suitable for use in SMBG. The present invention provides a flavin-bound glucose dehydrogenase having the following characteristics (1) to (5): (1) Temperature stability: stable at a temperature of 45° C. or lower; (2) stable at a pH range of 4.5 to 7.5; (3) substrate specificity: the reactivity to D-xylose, maltose, or D-galactose is 2% or less, based on the reactivity to D-glucose taken as 100%; (4) optimal activity temperature: 34 to 47° C.; and (5) optimal activity pH: 6.3 to 6.7.

The present invention provides a novel glucose dehydrogenase that has excellent substrate specificity and that is suitable for use in SMBG. The present invention provides a flavin-bound glucose dehydrogenase having the following characteristics (1) to (5): (1) Temperature stability: stable at a temperature of 45° C. or lower; (2) stable at a pH range of 4.5 to 7.5; (3) substrate specificity: the reactivity to D-xylose, maltose, or D-galactose is 2% or less, based on the reactivity to D-glucose taken as 100%; (4) optimal activity temperature: 34 to 47° C.; and (5) optimal activity pH: 6.3 to 6.7.

The disclosure discloses an enzyme electrode comprising; an electrode comprising a current collector; a monolayer-forming molecule bound to the surface of the current collector; and a glucose dehydrogenase comprising a cytochrome C subunit bound to the monolayer-forming molecule; wherein electrons are transferred between the glucose dehydrogenase and the current collector by oxidation-reduction reaction of the glucose dehydrogenase.

The disclosure discloses an enzyme electrode comprising; an electrode comprising a current collector; a monolayer-forming molecule bound to the surface of the current collector; and a glucose dehydrogenase comprising a cytochrome C subunit bound to the monolayer-forming molecule; wherein electrons are transferred between the glucose dehydrogenase and the current collector by oxidation-reduction reaction of the glucose dehydrogenase.

The present invention relates to a composition for the stabilization of glucose, lactate and homocysteine in blood after collection, to a use of the provided compositions and a method for the stabilization of glucose, lactate and homocysteine in blood after collection, as well as optionally the in vitro determination of glucose, lactate and homocysteine in blood, and a blood collection device provided for said use and method.