Abstract: A fusion protein of pyrroloquinoline quinone glucose dehydrogenase (PQQGDH) and a cytochrome is disclosed. PQQGDH is, for example, a water-soluble PQQGDH derived from Acinetobacter calcoaceticus. The cytochrome is, for example, an electron transfer domain of quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. The fusion protein of the present invention shows intramolecular electron transfer from PQQ, a redox center, to the cytochrome, which allow construction of a direct electron transfer-type glucose sensor which requires no electron mediators.

Abstract: Disclosed is a mutant human ?-synuclein with decreased ability of forming aggregation. The mutant human ?-synuclein of the invention is able to inhibit aggregation of the wild type human ?-synuclein, Ala53Thr mutant human ?-synuclein or Ala50Pro mutant human ?-synuclein, thus is useful for investigation of pathology and treatment of Parkinson's disease and for research and development of gene therapy. Also disclosed is a partial structure peptide of human ?-synuclein comprising amino acid substitutions as taught by the invention.

Abstract: Disclosed is a modified glucose dehydrogenase having pyrroloquinoline quinone as a coenzyme, wherein one or more amino acid residues in a region of amino acid 349-377 of water-soluble PQQGDH derived from Acinetobacter calcoaceticus is replaced with other amino acid residues and has an inhibition constant (Ksi) of 200 mM or more. The modified water-soluble PQQGDH of the invention can be utilized for measuring glucose levels in the presence of high concentrations of glucose because of the low substrate inhibition by glucose.

Abstract: Disclosed is a water-soluble PQQGDH wherein two subunits are linked together via a disulfide bond. The water-soluble PQQGDH of the invention exhibits improved thermal stability.

Abstract: The present invention provides synthetic polymers having novel catalytic functions which mimic enzymatic reactions. The invention also provides a method for measuring glycated proteins such as glycated hemoglobin (HbA1c) and glycated albumin and for measuring their decomposition products fructosylamines, such as fructosylvaline, as well as assay reagents and sensors for use in the method.

Abstract: Disclosed is a modified glucose dehydrogenase having pyrroloquinoline quinone as a coenzyme, wherein one or more amino acid residues in a region of 186-206 amino acid of water-soluble PQQGDH derived from Acinetobacter calcoaceticus or in an equivalent region from other species are replaced with other amino acid residues. Also disclosed is a gene coding for the modified glucose dehydrogenase of the invention, a vector comprising the gene of the invention and a transformant comprising the vector, as well as a glucose assay kit and a glucose sensor comprising the modified glucose dehydrogenase of the invention.

Abstract: The present invention relates to a glucose sensor (2) including an electrode (32) which includes a conductive component and glucose dehydrogenase immobilized to the conductive component. As the glucose dehydrogenase, use is made of a protein complex including a catalytic activity subunit which has glucose dehydrogenase activity, and an electron mediator subunit for supplying an electron donated from the catalytic activity subunit to the conductive component. Preferably, the glucose sensor (2) is designed to continuously measure the glucose level or successively measure the glucose level a plurality of times.

Abstract: Disclosed is a modified glucose dehydrogenase having pyrroloquinoline quinone as a coenzyme, wherein one or more amino acid residues in a region of 186-206 amino acid of water-soluble PQQGDH derived from Acinetobacter calcoaceticus or in an equivalent region from other species are replaced with other amino acid residues. Also disclosed is a gene coding for the modified glucose dehydrogenase of the invention, a vector comprising the gene of the invention and a transformant comprising the vector, as well as a glucose assay kit and a glucose sensor comprising the modified glucose dehydrogenase of the invention.

Abstract: A DNA fragment encoding a ? subunit is obtained by inverse PCR using primers designed based on the nucleotide sequnece of a N-terminal signal sequence region of a GDH ? subunit derived from Burkholderia cepacia KS1 strain.

Abstract: A DNA fragment encoding a ? subunit is obtained by inverse PCR using primers designed based on the nucleotide sequnece of a N-terminal signal sequence region of a GDH ? subunit derived from Burkholderis cepacia KS1 strain.

Abstract: A DNA fragment encoding a ? subunit is obtained by inverse PCR using primers designed based on the nucleotide sequence of a N-terminal signal sequence region of a GDH ? subunit derived from Burkholderia cepacia KS1 strain.

Abstract: Modified water-soluble glucose dehydrogenase having pyrrolo-quinoline quinone as a coenzyme are provided wherein at least one amino acid residue is replaced by another amino acid residue in a specific region. Modified water-soluble PQQGDHs of the present invention have improved thermal stability.

Abstract: Modified water-soluble glucose dehydrogenases having pyrrolo-quinoline quinone as a coenzyme are provided wherein at least one amino acid residue is replaced by another amino acid residue in a specific region. Modified water-soluble PQQGDHs of the present invention have improved affinity for glucose.

Abstract: Modified water-soluble glucose dehydrogenase having pyrrolo-quinoline quinone as a coenzyme are provided wherein at least one amino acid residue is replaced by another amino acid residue in a specific region. Modified water-soluble PQQGDHs of the present invention have improved thermal stability.

Abstract: Disclosed is a modified glucose dehydrogenase having pyrroloquinoline quinone as a coenzyme, wherein one or more amino acid residues in a region of amino acid 349-377 of water-soluble PQQGDH derived from Acinetobacter calcoaceticus is replaced with other amino acid residues and has an inhibition constant (Ksi) of 200 mM or more. The modified water-soluble PQQGDH of the invention can be utilized for measuring glucose levels in the presence of high concentrations of glucose because of the low substrate inhibition by glucose.

Abstract: Modified water-soluble glucose dehydrogenases having pyrrolo-quinoline quinone as a coenzyme are provided wherein at least one amino acid residue is replaced by another amino acid residue in a specific region. Modified water-soluble PQQGDHs of the present invention have improved affinity for glucose.

Abstract: A DNA fragment encoding a ? subunit is obtained by inverse PCR using primers designed based on the nucleotide sequnece of a N-terminal signal sequence region of a GDH ? subunit derived from Burkholderia cepacia KS1 strain.

Abstract: Disclosed is an enzyme electrode having an oxidoreductase (for instance, glucose oxidase, cholesterol oxidase, fructosylamine oxidase and glucose dehydrogenase) and an electron-transfer protein (for instance, cytochrome C, cytochrome b562 and cytochrome c551), as well as a sensor utilizing the enzyme electrode as working electrode. The enzyme electrode of the invention can provide high response current values.

Abstract: A modified glucose dehydrogenase is disclosed which comprises a water-soluble glucose dehydrogenase having a pyrroloquinoline quinone as a coenzyme. At least one amino acid residue present on the surface of the water-soluble glucose dehydrogenase is replaced with arginine. The side chain of the amino acid residue is exposed at the surface of the molecule and is not expected to substantially interact with other residues. The amino acid residue is present in a region that is probably not an enzyme active site or a substrate binding site. Preferably the amino acid residue is selected from the group consisting of glutamine, asparagine, and threonine. This modified enzyme can be prepared by recombinant processes and recovered efficiently.

Abstract: Disclosed is a water-soluble PQQGDH wherein two subunits are linked together via a disulfide bond. The water-soluble PQQGDH of the invention exhibits improved thermal stability.