Abstract: To provide a fuel cell that can perform efficient power generation through a simple fuel supply. There is provided a fuel cell that generates electricity through progress of an oxidation-reduction reaction using an enzyme as a catalyst, the fuel cell including at least a fuel-vaporizing layer formed through vaporization of a fuel; an anode to which a vaporized fuel is supplied from the fuel-vaporizing layer; and a cathode connected to the anode in a state in which protons can be conducted. In the fuel cell, since a fuel is supplied to an electrode in a vaporized state, a vaporized fuel is supplied to an inner portion of the electrode and a reaction sufficiently proceeds at the inner surface of the electrode, which can achieve high output due to efficient power generation.

Abstract: An objective of the present invention is to provide immunoassay microchips in which microstructures of beads having a sufficient reaction area were constructed within microchannels while suppressing flow path resistance, and to provide simple and highly-sensitive immunoassay methods for microsamples. The objective was achieved by immunoassay microchips comprising microchannels with microstructures arranged in at least a portion of the microchannels, the microstructures retaining microbeads uniformly dispersed in photo-cured hydrophilic resins, and the microbeads having a primary antibody immobilized on their surfaces, and by immunoassay methods using the microchips.

Abstract: In the case in which a fuel cell has a structure in which a cathode (2) and an anode (1) are opposed with the intermediary of an electrolyte layer (3) and the cathode (2) is formed of an electrode to which an oxygen reductase and so on is immobilized and this electrode has pores inside, at least part of the surface of this electrode is rendered water repellent. For example, the surface of the electrode is rendered water repellent by forming a water-repellent agent on the surface of this electrode. Thereby, in the case in which the cathode is formed of an electrode to which an enzyme is immobilized and this electrode has pores inside, a fuel cell that can stably achieve a high current value by optimization of the amount of water contained in the cathode and a manufacturing method thereof are provided.

Abstract: An enzyme-immobilized electrode is provided and includes an electrode composed of porous carbon or the like, a phospholipid layer on the electrode (11), and enzymes immobilized onto the phospholipid layer. The enzymes are, for example, diaphorase and glucose dehydrogenase. An intermediate layer composed of a protein or the like may be provided between the electrode and the phospholipid layer. By using the enzyme-immobilized electrode as a negative electrode or a positive electrode in a fuel cell using an enzyme, one or a plurality of types of enzymes can be immobilized at optimal positions on the electrode, and thus, there are provided a highly efficient enzyme-immobilized electrode and a highly efficient fuel cell using the enzyme-immobilized electrode.

Abstract: Antibody-containing solution formulations including a sugar as a stabilizer. Said solution formulations can further include a surfactant as a stabilizer.

Abstract: A method of quantifying an ethylene oxide based nonionic surfactant in a sample containing a physiologically active protein, characterized in that quantitation is performed by colorimetry, in particular, a method of quantifying an ethylene oxide based nonionic surfactant in a sample containing a physiologically active protein, characterized in that an ammonium thiocyanate/cobalt nitrate reagent (CoSCN reagent) is added to said sample solution and the resulting cobalt thiocyanate complex is quantified by absorbance measurement.

Abstract: A method for manufacturing a fuel cell having a structure in which a positive electrode and a negative electrode are opposed with a proton conductor therebetween and an enzyme is immobilized on the positive electrode and/or the negative electrode includes the step of immobilizing the enzyme on the positive electrode and/or the negative electrode with a photo-curable resin and/or a thermosetting resin. A photo-curable resin and/or a thermosetting resin may be further laminated on the photo-curable resin and/or the thermosetting resin which have immobilized the enzyme.

Abstract: Antibody-containing solution formulations including a sugar as a stabilizer. Said solution formulations can further include a surfactant as a stabilizer.

Abstract: A method of quantifying an ethylene oxide based nonionic surfactant in a sample containing a physiologically active protein, characterized in that quantitation is performed by colorimetry, in particular, a method of quantifying an ethylene oxide based nonionic surfactant in a sample containing a physiologically active protein, characterized in that an ammonium thiocyanate/cobalt nitrate reagent (CoSCN reagent) is added to said sample solution and the resulting cobalt thiocyanate complex is quantified by absorbance measurement.

Abstract: A method for assaying the binding activity of a first ligand to a chemically less stable ligand-binding protein, comprising immobilizing a second ligand that binds to the ligand-binding protein at a binding site distinct from the binding site of the first ligand to the ligand-binding protein, binding the protein to the second ligand, and then measuring the binding activity of the first ligand to the protein via surface plasmon resonance.

Abstract: The present invention provides stabilized preparations containing an antibody in a glycine buffer and/or a histidine buffer and also provides processes for preparing a protein-containing stabilized preparation, comprising adjusting the pH with a basic amino acid or a basic amino acid derivative or a salt thereof.

Abstract: The present invention provides a convenient and highly accurate method of measuring the biological activity of a ligand. Namely, this method of evaluating the binding activity of a ligand to a ligand-binding protein comprises; measuring the binding activity value of the ligand to the ligand-binding protein, and measuring the binding activity value of the above-described ligand to a second ligand-binding substance binding to a site other than the binding site where the ligand binds to the above-described ligand-binding protein.