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公开(公告)号:JP2007000038A
公开(公告)日:2007-01-11
申请号:JP2005181506
申请日:2005-06-22
Applicant: TORAY INDUSTRIES
Inventor: ISHII KENTARO , MIWA TAKASHI , KONDO TETSUJI
IPC: C12M1/36
Abstract: PROBLEM TO BE SOLVED: To provide a closed-system circulatory circuit-type culturing device solving the following problems: in a conventional closed-system circulatory circuit-type culturing device, it is impossible to keep pH constant through controlling optimum culturing environment according to cell proliferation only by gas exchange; insertion of a lot of sensors results in being at high risk of interfusion of foreign matters; and it is necessary to make all the part getting in touch with blood disposable for being used for curing for medical use because use of an identical sensor to different patients has a risk of infection. SOLUTION: The closed-system circulatory circuit-type culturing device controls pH of culture soil in a culture soil reservoir with acidic gas so as to keep pH of the culture soil constant, detects deterioration in the culture soil based on addition of the acidic gas to be controlled so as to determine the time to exchange culture soil only with a pH sensor, and employs a noncontact-type pH sensor not directly getting in touch with the culture soil so as to eliminate the need for making the sensor disposable. COPYRIGHT: (C)2007,JPO&INPIT
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公开(公告)号:JP2003174886A
公开(公告)日:2003-06-24
申请号:JP2001378421
申请日:2001-12-12
Applicant: TORAY INDUSTRIES
Inventor: UCHIYAMA TAKEHIKO , AKIYAMA TORU , MIWA TAKASHI , SHIBAYAMA NAOKO
IPC: C12N15/09 , C07K14/315 , C07K19/00 , C12P21/02
Abstract: PROBLEM TO BE SOLVED: To provide a new protein having superantigenicity derived from Streptococcus dysgalactiae, a DNA encoding the protein and a method for purifying the protein. SOLUTION: This protein comprises the same or substantially the same amino acid sequence as a specific amino acid sequence derived from the Streptococcus dysgalactiae. The DNA encodes the protein. COPYRIGHT: (C)2003,JPO
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公开(公告)号:JP2000245831A
公开(公告)日:2000-09-12
申请号:JP5551699
申请日:1999-03-03
Applicant: TORAY INDUSTRIES
Inventor: SAKAI RUMIKO , MIWA TAKASHI , FUKUYAMA MAYUMI
IPC: A61M1/36
Abstract: PROBLEM TO BE SOLVED: To detoxicate or remove quickly the toxin activity of myoglobins by using a material containing one chemical structure selected from a urea bond, a thiourea bond and an amide bond for a drug that remove the toxin activity of myoglobin existing in a high concentration protein solution such as blood or the like. SOLUTION: A matter useful for detoxication or removal of myoglobins that escape easily from cells and flow into blood due to the melting and necrosis of myocytes due mainly to the compression of an external force is prepared from one containing at least one selected from a urea bond, thiourea bond and an amide bond. As a substituent that bonds with at least one kind selected from among the urea bond, thiourea bond and amide bond, a structure having a functional group that can form a hydrogen bond such as an amino group, hydroxy group, carboxy group or the like is used preferentially, and as a structure having an amino group for example, a compound (polyamine) having a plurality of amino groups such as aminohexane, monomethylaminohexane or the like is used.
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公开(公告)号:JPH10147541A
公开(公告)日:1998-06-02
申请号:JP30805396
申请日:1996-11-19
Applicant: TORAY INDUSTRIES
Inventor: FUKUYAMA MAYUMI , MIWA TAKASHI , SAKAI RUMIKO
IPC: A61K47/48 , A61K31/715 , A61K31/74 , A61P31/04
Abstract: PROBLEM TO BE SOLVED: To obtain the subject material having excellent selective affinity to super-antigen even in a neutral solution having high protein concentration, enabling disinfection treatment and producible at a low cost by introducing a group capable of forming hydrogen bond. SOLUTION: The objective material for the removal or detoxication of super- antigen is produced by introducing at least one group capable of forming hydrogen bond [excluding (thio)urea bond] into a monomer, an oligomer or a polymer. The group capable of forming hydrogen bond is e.g. amide group, amino group, hydroxyl group, carboxyl group, aldehyde group or mercapto group and it is preferable that the material contains at least one amide group. The introduction of a group capable of forming hydrogen bond can be carried out by conventional methods. For example, in the case of introducing amide group into an aliphatic compound or an aromatic compound, an acid chloride or an acid anhydride is made to react with an amino compound.
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公开(公告)号:JPH1085330A
公开(公告)日:1998-04-07
申请号:JP24608096
申请日:1996-09-18
Applicant: TORAY INDUSTRIES
Inventor: MIWA TAKASHI , SHIMIZU SHINJI , SAKAI RUMIKO
Abstract: PROBLEM TO BE SOLVED: To obtain a material having a less affinity to useful constituents contained in blood, medicines and the like, and having an affinity to bacterial pyrogen of protein, such as staphylococcus aureus exotoxin and so forth, but not limiting to endotoxin, by containing urea or thiourea bond. SOLUTION: The substance to remove or detoxificate pyrogen that is produced by Gram-negative or Gram-positive bacteria, is manufactured from a material containing urea or thiourea bond. In this case, as a substittion group to be joined with urea or thiourea bond, such aliphatic compounds as hexyl group, octyl group, dodecyl group and the like, and such alicyclic compounds as cyclohexane, cyclopentane and the like, are used. Most preferably, however, are those having compounds both with aromatic family compounds and hydroxyl or amino group as a group substituting for urea or thiourea bond.
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公开(公告)号:JPH08283300A
公开(公告)日:1996-10-29
申请号:JP8949495
申请日:1995-04-14
Applicant: TORAY INDUSTRIES
Inventor: MIWA TAKASHI , FUKUYAMA MAYUMI , ISHIKAWA KAZUO
IPC: C12N15/09 , A61K39/00 , A61P37/00 , C07K17/08 , C07K17/10 , C07K17/12 , C07K17/14 , C07K19/00 , C12P21/02 , C12R1/19
Abstract: PURPOSE: To obtain a fused protein having super-antigen binding capacity, T-cell activation capacity, etc., and useful as an immobilization material for protein, etc., by fusing the α-subunit of a major histocompatibility antigen class II protein or a part of the α-subunit with the β-subunit or a part of the β- subunit. CONSTITUTION: This new fused protein having improved productivity and handleability while keeping the functions of a major histocompatibility antigen (MHC) class II, producible without using a crosslinking operation after immobilization, having functions of super-antigen binding capacity, T-cell activation capacity, etc., and useful e.g. as a fused cell immobilization material for the removal, detection, etc., of super-antigen is produced by fusing the MHC class II protein α-subunit or a part of the α-subunit with β-subunit or a part of the β-subunit. The fused protein can be produced by inserting a DNA coding for the 1st to 80th amino acid residues of the MHC class II α-subunit into a vector, inserting a DNA coding for a sequence having Gly-Tnbr-Ser-Gly as a spacer at the N-terminal of the β-subunit into the vector and expressing the vector in a host cell.
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公开(公告)号:JPH04102065A
公开(公告)日:1992-04-03
申请号:JP22048190
申请日:1990-08-21
Applicant: TORAY INDUSTRIES
Inventor: MIWA TAKASHI , SHOJI HISANORI
IPC: G01N33/579
Abstract: PURPOSE:To enable determination of accurate endotoxin concentration by deactivating reaction preventing factors and facilitating factors in solution by means of dilution heating or perchloric acid treatment and by creating a calibration curve with influence of various kinds of factors in the solution offset. CONSTITUTION:Change in time required to be gel is observed in a nethelometric time analysis method as a measurement method. Time T0 required to be gel as to a specimen to be determined is measured from time change data of a ratio in transmitted light amounts. Then time periods required for specimen with endotoxin solution of known concentrations added to be gel are measured, which refer to T1, T2... Tn (n>=2). The solution concentration is adjusted to solution concentration C1, C2... Cn by adding the endotoxin solution of known concentrations to the specimen, and calibration curves with time T1, T2... Tn (n>=2) required to be gel which is measured in respective solution are created, while a concentration C0 is obtained from time T0 required to be gel based on the calibration curves. Then, by using C1+C0, C2+C0,... Cn+C0 wherein C0 is added to each of C1, C2... Cn and T1, T2... Tn to obtain a calibration curve again, operation for recalculating C0 from T0 is performed.
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