Abstract: An additive of the formula (1) for use in electrolytic solutions wherein A is —CH(X)— or —C?C(X)—, X being hydrogen, halogen, alkyl having 1 to 4 carbon atoms, alkoxycarbonyl having 2 to 5 carbon atoms, benzoyl or alkoxycarbonylalkyl having 3 to 9 carbon atoms, Q1 and Q2 are the same or different and are each alkyl having 1 to 6 carbon atoms, alkoxyl having 1 to 4 carbon atoms, alkoxycarbonylalkyl having 3 to 9 carbon atoms or amino having as a substituent alkyl having 1 to 4 carbon atoms, and A, Q1 and Q2 may form a ring structure.

Abstract: The object of the present invention is to provide a novel trehalose compound having a high affinity for an adenosine A3 receptor. The trehalose compound of the present invention is represented by General Formula (1): wherein X and X? represent a hydrogen atom, and the like; Y and Y? independently represent an oxygen atom, and the like; R1 and R2 independently represent a C1-C6 alkyl group; and R3 and R4 independently represent a C3-C6 alkyl group. The trehalose compound of the present invention has a remarkably high affinity for an adenosine A3 receptor.

Abstract: An asparagine-linked ?2,3-oligosaccharide having undeca- to hepta-saccharides, an asparagine-linked ?2,6-oligosaccharide having undeca- to hepta-saccharides and containing fluorine and an asparagine-linked oligosaccharide derivative containing at least one fucose in N-acetylglucosamine on the nonreducing terminal side of an asparagine-linked oligosaccharide wherein the asparagine has amino group protected with a lipophilic protective group, and a process for producing these compounds.

Abstract: Disclosed is a polypeptide having an enhanced effector function. Specifically disclosed are: a polypeptide having a modified Fc region; a nucleic acid encoding the polypeptide; a vector carrying the nucleic acid; a host cell or a host organism harboring the vector; a pharmaceutical composition comprising the polypeptide; a method for producing the polypeptide; a method for enhancing the effector function of an antibody; and a method for producing a cell capable of producing an antibody having a high effector function.

Abstract: Glycopeptide having at least one asparagine-linked oligosaccharide at a desired position of the peptide chain obtained by: (1) esterifying hydroxyl of a resin and carboxyl of an amino acid having amino group nitrogen protected with a fat-soluble protective group (AGFPG), (2) removing the protective group to form a free amino group, (3) amidating the free amino group and carboxyl of an amino acid having AGFPG, (4) removing the protective group, (5) repeating the steps (3) and (4), (6) amidating the free amino group and carboxyl of the asparagine portion of an asparagine-linked oligosaccharide having AGFPG, (7) removing the protective group, (8) amidating the free amino group and carboxyl of an amino acid having AGFPG, (9) repeating steps (7) and (8), (10) removing the protective group, and (11) cutting off the resin with an acid; glycopeptide obtained by transferring sialic acid or a derivative thereof to the above glycopeptide.

Abstract: An object of the invention is to provide a novel sphingosine compound with an inhibitory activity against sphingomyelinase, and a method for producing the sphingosine compound. The novel sphingosine compound or a salt thereof according to the invention is represented by Formula (1): wherein one of R1 and R2 is hydrogen, and the other is a group represented by Formula (G): wherein n is 0 or 1; and R3 is hydrogen, C1-23 alkyl, C3-8 cycloalkyl, C2-6 alkenyl, C1-6 alkoxy, C3-8 cycloalkyloxy, phenyl, or furil.

Abstract: A full-length IgG-Fc fragment having a substantially homogeneous sugar chain added thereto, and a process for producing the full-length IgG-Fc fragment. Specifically, an IgG-Fc fragment has a sugar chain added thereto, in which the sugar chain is added to the same position as that in a naturally occurring IgG-Fc fragment, any one amino acid residue selected from 1st to 30th amino acid residues from the sugar chain-added amino acid residue on the N-terminal side of the sugar chain-added amino acid residue is substituted by a Cys residue and at least one Met reside is substituted by an amino acid reside other than a Met residue.

Abstract: Disclosed is a promoter which enables the expression of a gene product in a large quantity in Bacillus subtilis. Also disclosed is a method for producing a gene product using the promoter. Specifically disclosed are: a nucleic acid molecule which contains a promoter region derived from a toxin gene of a bacterium belonging to the genus Clostridium and can enhance the expression of a heterologous gene operably linked to the nucleic acid molecule; a nucleic acid construct which contains the nucleic acid molecule and the heterologous gene; a vector carrying the nucleic acid construct; a host cell which is transformed with the vector; and a method and a kit for producing an expression product of the heterologous gene using the nucleic acid molecule, the nucleic acid construct, the vector or the host cell.

Abstract: An organobismuth compound represented by the formula (1) and a method for preparing a living radical polymer using the organobismuth compound. In the formula (1), R1 to R3 each represent a C1-C8 alkyl group, an aryl group, a substituted aryl group, an aromatic heterocyclic group or a group represented by the formula (2) where at least one of R1 to R3 is a group represented by the formula (2), wherein R4 and R5 each represent a C3-C8 alkyl group, an aryl group or a substituted aryl group, and R6 to R8 each represent a hydrogen atom, a C1-C8 alkyl group, an aryl group or a substituted aryl group.

Abstract: Glycopeptide having at least one asparagine-linked oligosaccharide at a desired position of the peptide chain obtained by: (1) esterifying hydroxyl of a resin and carboxyl of ah amino acid having amino group nitrogen protected with a fat-soluble protective group (AGFPG), (2) removing the protective group to form a free amino group, (3) amidating the free amino group and carboxyl of an amino acid having AGFPG, (4) removing the protective group, (5) repeating the steps (3) and (4), (6) amidating the free amino group and carboxyl of the asparagine portion of an asparagine-linked oligosaccharide having AGFPG, (7) removing the protective group, (8) amidating the free amino group and carboxyl of an amino acid having AGFPG, (9) repeating steps (7) and (8), (10) removing the protective group, and (11) cutting off the resin with an acid; glycopeptide obtained by transferring sialic acid or a derivative thereof to the above glycopeptide.

Abstract: A low-molecular-weight polysulfated hyaluronic acid derivative useful for prevention and/or treatment of an allergic disease. An agent for prevention and/or treatment of an allergic disease selected from pollinosis, allergic rhinitis, allergic conjunctivitis, atopic dermatitis, and asthma, represented by the following general formula (IA) or (IB); wherein n represents a number of 0 to 15; R?s each independently represent a hydrogen atom or an SO3H group etc.

Abstract: The present invention provides a process for producing a peptide thioester compound. The process involves: (A) forming a peptide by a solid-phase synthesis method using a resin modified with a linker represented by the formula (1) as a solid phase: wherein R1 represents C1-4 alkyl group, R2 represents hydrogen atom or C1-4 alkoxy group, and n represents an integer of 1 to 4; (B) cleaving a bond between the solid phase and the peptide with at least one acid selected from dilute hydrochloric acid, dilute sulfuric acid, formic acid, and acetic acid to produce a peptide having a carboxyl group at the C-terminus; and (C) reacting a thiol compound with the peptide at ?100 to 0° C. in the presence of a condensing agent in a solvent.

Abstract: A method for producing a glycoprotein, which is uniform in terms of functions derived from a sugar chain (e.g., a blood half-life) and physiological activities, i.e., a glycoprotein, which is uniform in terms of the amino acid sequence, the sugar chain structure and the higher-order structure; specifically, a method for producing a glycoprotein, which is uniform in terms of the amino acid sequence, the sugar chain structure, and the higher-order structure, includes the following steps (a) to (c): (a) folding a glycoprotein, which is uniform in terms of the amino acid sequence and the sugar chain structure; (b) fractionating the folded glycoprotein by column chromatography; and (c) collecting a fraction having a specified activity.

Abstract: A process for preparing a highly pure quaternary ammonium salt comprising: (1) adding a quaternary ammonium hydroxide salt or quaternary ammonium carbonate to a quaternary ammonium salt containing a protonic acid salt of a tertiary amine as an impurity and thereby neutralizing the tertiary amine protonic acid salt with the quaternary ammonium hydroxide salt or carbonate to convert the acid salt to a tertiary amine and water and to convert the quaternary ammonium hydroxide salt or carbonate to a quaternary ammonium salt at the same time, and (2) removing the tertiary amine and water produced from the system.

Abstract: A process for preparing a high-purity quaternary ammonium salt comprising: (1) adding an oxide or hydroxide of a Group 1, 2, 12 or 13 metal to a quaternary ammonium salt containing a protonic acid salt of a tertiary amine as an impurity and thereby neutralizing the tertiary amine protonic acid salt with the metal oxide or hydroxide to convert the acid salt to a tertiary amine and water and to convert the metal oxide or hydroxide to a metal salt at the same time, and (2) removing the tertiary amine, water and metal salt produced from the system.

Abstract: Provided are a method of producing a graft copolymer, the method involving subjecting a radically polymerizable monomer to living radical graft polymerization with a rubber component formed of a natural rubber and/or a synthetic diene-based rubber in an aqueous medium in the presence of a polymerization control agent, a rubber composition containing the graft copolymer obtained by the method, and a tire obtained by using the rubber composition in any one of its tire members.

Abstract: A trehalose compound having high immunopotentiating activity and low toxicity is represented by formula (1). (In the formula, X and X? each represents a phenyl, a naphthyl, R1—CHR1— (wherein R1 and R2 each represents a C7-C21 alkyl group or the like) or the like; and n and n? each independently represents an integer of 0-3). The compound exhibits a high activating effect on macrophages and neutrophils.

Abstract: An organoantimony compound represented by the formula (1), processes for producing polymers with use of the compound, and polymers wherein R1 and R2 are C1-C8 alkyl, aryl, substituted aryl or an aromatic heterocyclic group, R3 and R4 are each a hydrogen atom or C1-C8 alkyl, and R5 is aryl, substituted aryl, an aromatic heterocyclic group, oxycarbonyl or cyano.

Abstract: Oligosaccharide chain added GLP-1 peptides are more stable in blood and more active in controlling blood-sugar levels than GLP-1 peptides without added oligosaccharides. Oligosaccharide chain added GLP-1 peptides having GLP-1 activity include at least one or at least two amino acids each substituted with an oligosaccharide chain added amino acid in GLP-1; a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or a GLP-1 analog. Oligosaccharide chain added GLP-1 peptides with at least one amino acid substituted with an oligosaccharide chain added amino acid include an oligosaccharide chain with oligo hyaluronic acid. Oligosaccharide chain added amino acids include oligosaccharide chains attached to amino acids via linkers.

Abstract: The present invention provides a method for producing a peptide, characterized in that it comprises converting an —SH group of a peptide comprising an amino acid residue having the —SH group to an —OH group, wherein said method comprises the following steps (a) to (c): (a) allowing an —SH group in a peptide to react with a methylating agent to convert the —SH group to an —SMe group; (b) allowing the —SMe group obtained in the step (a) to react with a cyanizing agent to produce a reaction intermediate; and (c) converting the reaction intermediate obtained in the step (b) to a peptide comprising an amino acid residue having an —OH group under more basic conditions than the conditions in the step (b).