Patent application number | Description | Published |
20090269235 | Production method for sintered machine components - A production method for sintered machine components, includes preparing an Fe alloy powder A, an Fe alloy powder B, an Fe—P powder, and a graphite powder. The Fe alloy powder A consists of, by mass %, 25 to 45% of Cr, 1.0 to 3.0% of Mo, 1.0 to 3.0% of Si, 0.5 to 1.5% of C, and the balance of Fe and inevitable impurities. The Fe alloy powder B consists of, by mass 15 to 35% of Cr, 15 to 30% of Ni, and the balance of Fe and inevitable impurities, and the Fe—P powder consists of 10 to 30 mass % of P and the balance of Fe and inevitable impurities. The production method further includes mixing 40 to 60 mass % of the Fe alloy powder B, 1.0 to 5.0 mass % of the Fe—P powder, and 0.5 to 3.5 mass % of the graphite powder with the Fe alloy powder A into a mixed powder. The production method further includes compacting the mixed powder into a green compact and sintering the green compact. | 10-29-2009 |
20130058825 | SINTERED ALLOY AND MANUFACTURING METHOD THEREOF - A sintered alloy includes, in percentage by mass, Cr: 11.75 to 39.98, Ni: 5.58 to 24.98, Si: 0.16 to 2.54, P: 0.1 to 1.5, C: 0.58 to 3.62 and the balance of Fe plus unavoidable impurities; a phase A containing precipitated metallic carbides with an average particle diameter of 10 to 50 μm; and a phase B containing precipitated metallic carbides with an average particle diameter of 10 μm or less, wherein the phase A is randomly dispersed in the phase B and the average particle diameter DA of the precipitated metallic carbides in the phase A is larger than the average particle diameter DB of the precipitated metallic carbides of the phase B. | 03-07-2013 |
20130084203 | IRON-BASED SINTERED SLIDING MEMBER AND PRODUCTION METHOD THEREFOR - An iron-based sintered sliding member consists of, by mass %, 0.1 to 10% of Cu, 0.2 to 2.0% of C, 0.03 to 0.9% of Mn, 0.52 to 6.54% of S, and the balance of Fe and inevitable impurities. The iron-based sintered sliding member satisfies the following First Formula in which [S %] represents mass % of S and [Mn %] represents mass % of Mn in the overall composition. The iron-based sintered sliding member exhibits a metallic structure in which pores and sulfide particles are dispersed in the matrix that includes a martensite structure at not less than 50% by area ratio in cross section. The sulfide particles are dispersed at 3 to 30 vol. % with respect to the matrix. | 04-04-2013 |
20130251585 | SINTERED ALLOY AND PRODUCTION METHOD THEREFOR - A sintered alloy has an overall composition consisting of, by mass %, 13.05 to 29.62% of Cr, 6.09 to 23.70% of Ni, 0.44 to 2.96% of Si, 0.2 to 1.0% of P, 0.6 to 3.0% of C, and the balance of Fe and inevitable impurities; a metallic structure in which carbides are precipitated and uniformly dispersed in an iron alloy matrix having dispersed pores; and a density of 6.8 to 7.4 Mg/m | 09-26-2013 |
20140248174 | SINTERED ALLOY AND MANUFACTURING METHOD THEREOF - A sintered alloy includes, in percentage by mass, Cr: 10.37 to 39.73, Ni: 5.10 to 24.89, Si: 0.14 to 2.52, Cu: 1.0 to 10.0, P: 0.1 to 1.5, C: 0.18 to 3.20 and the balance of Fe plus unavoidable impurities; a phase A containing precipitated metallic carbide with an average particle diameter of 10 to 50 μm; and a phase B containing precipitated metallic carbide with an average particle diameter of 10 μm or less, wherein the phase A is randomly dispersed in the phase B and the average particle diameter DA of the precipitated metallic carbide in the phase A is larger than the average particle diameter DB of the precipitated metallic carbide of the phase B. | 09-04-2014 |
20140271320 | IRON BASED SINTERED SLIDING MEMBER AND METHOD FOR PRODUCING SAME - An iron-based sintered sliding member is provided in which solid lubricating agent is dispersed uniformly inside of powder particles in addition to inside of pores and particle interfaces of the powder, the agent is strongly fixed, and sliding properties and mechanical strength are superior. The iron-based sintered sliding member contains S: 0.2 to 3.24 mass %, Cu: 3 to 10 mass %, remainder: Fe and inevitable impurities, as an overall composition; the metallic structure includes a base in which sulfide particles are dispersed, and pores; the base is a ferrite phase or a ferrite phase in which copper phase is dispersed; and the sulfide particles are dispersed at a ratio of 0.8 to 15.0 vol % versus the base. | 09-18-2014 |
20140286812 | IRON BASE SINTERED SLIDING MEMBER AND METHOD FOR PRODUCING SAME - An iron-based sintered sliding member is provided in which solid lubricating agent is dispersed uniformly inside of powder particles in addition to inside of pores and particle interfaces of the powder, the agent is strongly fixed, and sliding properties and mechanical strength are superior. The iron-based sintered sliding member contains S: 3.24 to 8.10 mass %, remainder: Fe and inevitable impurities, as an overall composition; the metallic structure includes a ferrite base in which sulfide particles are dispersed, and pores; and the sulfide particles are dispersed at a ratio of 15 to 30 vol % versus the base. | 09-25-2014 |
Patent application number | Description | Published |
20090137780 | METHOD FOR PRODUCTION OF PEPTIDE THIOESTER COMPOUND - The present invention provides a process for producing a peptide thioester compound, characterized by comprising: (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; (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: (1) wherein R | 05-28-2009 |
20100080794 | MUTANT POLYPEPTIDE HAVING EFFECTOR FUNCTION - Mutant polypeptides of the present invention contain an Fc region in which a cysteine residue is substituted for the second amino acid from the glycosylation site to the N terminal side in the Fc region. The Fc region is preferably a human IgG Fc region. The mutant polypeptides of the present invention may also contain an N-linked sugar chain at the glycosylation site in Fc region. Furthermore, a polypeptide domain other than the Fc region of the mutant polypeptides of the present invention may be a polypeptide molecule that recognizes a human cell surface molecule. | 04-01-2010 |
20100306864 | POLYPEPTIDE HAVING ENHANCED EFFECTOR FUNCTION - 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. | 12-02-2010 |
20110172392 | METHOD FOR PRODUCING PEPTIDE - 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). | 07-14-2011 |
20110313136 | IgG-Fc FRAGMENT AND PROCESS FOR PRODUCING THE SAME - 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. | 12-22-2011 |
20120047586 | POLYPEPTIDE HAVING ENHANCED EFFECTOR FUNCTION - 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. | 02-23-2012 |
20120114595 | SUGAR CHAIN-ADDED AILIM EXTRACELLULAR DOMAIN AND METHOD FOR PRODUCING SAME - Disclosed is a synthetic AILIM extracellular domain which has high ligand-binding ability and a quality sufficient for a pharmaceutical product. Also disclosed is a method for synthesizing the synthetic AILIM extracellular domain. Specifically disclosed is a sugar chaim-added AILIM extracellular domain wherein a sugar chain is bound at a position corresponding to the 69-position of the amino acid sequence of human AILIM extracellular domain, said amino acid sequence being depicted in SEQ ID NO: 7, and no sugar chain is added at positions corresponding to the 3-position and the 90-position of the amino acid sequence. | 05-10-2012 |
20140315800 | Glycosylated Polypeptide and Drug Composition Containing Said Polypeptide - [Problem] To provide a glycosylated polypeptide having affinity to somatostatin receptors and, compared to somatostatins, having improved in-blood stability. [Solution] The glycosylated polypeptide is characterized by at least two amino acids in a somatostatin or an analogue thereof being replaced by glycosylated amino acids. | 10-23-2014 |
20140336116 | Glycosylated Polypeptide and Drug Composition Containing Said Polypeptide - [Problem] To provide a glycosylated polypeptide having an affinity to somatostatin receptors, and, compared to somatostatins, having improved in-blood stability. [Solution] The glycosylated polypeptide is characterized by at least one amino acid in a somatostatin or an analog thereof being replaced with a glycosylated amino acid. | 11-13-2014 |
20140369964 | GLYCOSYLATED POLYPEPTIDE AND PHARMACEUTICAL COMPOSITION CONTAINING SAME - The object of the present invention is to provide a glycosylated polypeptide having uniform sugar chain structure which has interferon β activity. It was found that a glycosylated polypeptide having uniform sugar chain structure as well as having interferon β activity can be prepared by a method comprising a step of synthesizing a glycosylated peptide fragment and at least two peptide fragments and a step of linking the glycosylated peptide fragment and the at least two peptide fragments. | 12-18-2014 |
Patent application number | Description | Published |
20080214798 | Sugar chain asparagine derivatives, sugar chain asparagine, sugar chain and processes for producing these - An asparagine-linked α2,3-oligosaccharide having undeca- to hepta-saccharides, an asparagine-linked α2,6-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. | 09-04-2008 |
20090111739 | SUGAR CHAIN ADDED GLP-1 PEPTIDE - The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog. | 04-30-2009 |
20110195897 | GLYCOSYLATED GLP-1 PEPTIDE - 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. | 08-11-2011 |
20110245166 | SUGAR CHAIN ADDED GLP-1 PEPTIDE - The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog. | 10-06-2011 |
20110262945 | GLYCOPROTEIN PRODUCTION METHOD AND SCREENING METHOD - 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. | 10-27-2011 |
20130345129 | SUGAR CHAIN ADDED GLP-1 PEPTIDE - The present invention relates to an oligosaccharide chain added GLP-1 peptide that has higher stability in blood than that of GLP-1 and, preferably, exhibits higher activity of controlling blood-sugar levels than that of GLP-1. The present invention relates to an oligosaccharide chain added GLP-1 peptide having GLP-1 activity, wherein at least one amino acid is substituted with an oligosaccharide chain added amino acid, in: (a) GLP-1; (b) a peptide having the amino acid sequence of GLP-1 with deletion, substitution or addition of one or several amino acids; or (c) a GLP-1 analog. | 12-26-2013 |
20140235822 | METHOD FOR PRODUCING PEPTIDE - 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). | 08-21-2014 |