Kowa Company Limited

Teijin Limited

Hitachi, Ltd.

The Japan Carlit Co., Ltd.

Jx Nippon Oil Energy Corporation

Euglena Co., Ltd.

Kanto Koatsu

Nobuo Aoki

Yataro Ichikawa

Yoshihiko Sumi

Shigeru Kimura

Masami Shiratsuchi

Masami Muramatsu

Tetsuo Takematsu

Fusaji Shoji

Takashi Kaneko

Kengo Suzuki

Takao Nagoya

Yasutomo Takeuchi

Ryohei Nakano

Ken Amano

Yukiya Koike

Koichi Moriya

Tsuyoshi Aoyama

Ryo Arashida

Michiyuki Kohno

Yoichi Sakata

Akihiko Aoki

Kenji Wakabayashi

Yukio Fukushima

Shinichiro Kurosawa

Jun Mimuro

Iwao Ueda

Jun Kurita

Toshiyuki Kiriyu

Yoshinori Matsuzaki

Hiroaki Kato

Masami Murakami

Nobuhiko Yoshida

Ko Yamashita

Taro Tamaki

Toshiro Watanuki

The present invention provides a production method for biofuel based on a technology to convert carbon-dioxide as a carbon source through photosynthesis by photosynthetic microorganisms to biomass and produce biofuel of the biomass. The production method for biofuel of the present invention comprises a culturing process (S) of culturing in a culture solution photosynthetic microorganisms which store oils, fats and carbohydrates in cells of the photosynthetic microorganisms, an oil and fat conversion process (S) of converting the carbohydrates stored in the cells of the photosynthetic microorganisms cultured in the culture apparatus to oils and fats, an extraction process (S) of extracting the oils and fats out of the cells of the photosynthetic microorganisms, and a reforming process (S) to reform the extracted oils and fats.

Production method for biofuel

A protein having human plasmin inhibiting activity, substantially equivalent reactivity with human plasmin to a human .alpha..sub.2 -plasmin inhibitor derived from plasma, a binding ability to human fibrin about 1/4 to about 1/3 of that of the human .alpha..sub.2 -plasmin inhibitor derived from plasma, and a molecular weight of about 50,000 to about 77,000.

Protein having human plasmin inhibiting activity

This invention provides a monoclonal antibody or its fragment specific to a human .alpha..sub.2 -plasmin inhibitor, said antibody having the function of specifically blocking that site of the human .alpha..sub.2 -plasmin inhibitor which inhibits the fibrinolytic activity of plasmin, and of suppressing said fibrinolytic activity inhibiting function of said .alpha..sub.2 -plasmin inhibitor, and also a hybridoma capable of producing the monoclonal antibody. Said monoclonal antibody or its fragment is useful for the immunological determination of a human .alpha..sub.2 -plasmin inhibitor, the separation or recovery of a human .alpha..sub.2 -plasmin inhibitor from a liquid containing the human .alpha..sub.2 -plasmin inhibitor, and the treatment of a thrombotic disease.

Monoclonal antibody specific to human .alpha..sub.2 -plasmin inhibitor

cDNA encoding a human .alpha..sub.2 -plasmin inhibitor precursor protein represented by an amino acid sequence from the -39th Met to the 452nd Lys in FIG. 1 of the accompanying drawings; an amino acid sequence of a human .alpha..sub.2 -plasmin inhibitor precursor represented by an amino acid sequence from the -39th Met to the 452nd Lys in FIG. 1 of the accompanying drawings; and genomic DNA encoding a human .alpha..sub.2 -plasmin inhibitor protein which is composed of exons II, III, IV, V, VI, VII, VIII, IX and X in FIG. 4 of the accompanying drawings, said exons being bonded to one another via introns.

cDNA and genomic DNA encoding the amino acid sequence of human

The present invention provides a monoclonal antibody specific to a thrombin-binding substance (TM), hybridomas producing the monoclonal antibody, a purification process of TM featuring the use of the monoclonal antibody as an immunoadsorbent, as well as an immunoassay of TM featuring the use of the monoclonal antibody.

Anti-thrombin-binding substance monoclonal antibodies, hybridomas

Highly pure 3,3',4,4'-biphenyltetracarboxylic acid (BPTA) and dianhydride thereof (BPDA) are produced by heating crude BPTA to give BPDA, treating the BPDA with hot water to give highly pure BPTA, and in the case of highly pure BPDA, heat treating the pure BPTA to give highly pure BPDA.

Process for producing highly pure 3,3',4,4'-biphenyltetracarboxylic acid

Thrombin-binding substances are obtained by fractionating human urine by ion-exchange chromatography, affinity chromatography using a thrombin-bound carrier, immune adsorption column chromatography, gel filtration, and/or molecular-weight fractionation. One of the substances has a molecular weight of 46,500.+-.6,000 in reduced condition and 39,000.+-.10,000 in unreduced condition by SDS PAGE and an isoelectric point at pH 5.0-5.3, while the other has a molecular weight of 40,000.+-.8,000 in reduced condition and 31,000.+-.10,000 in unreduced condition by SDS PAGE and an isoelectric point at pH 4.9-5.7. They have strong affinity to thrombin. They are capable of promoting the thrombin catalyzed activation of protein C and prolong clotting time. They are stable to denaturing agents (urea and sodium dodecylsulfate).

Thrombin-binding substance and process for its preparation

Novel thrombin-binding substances (A) and (B) are disclosed. The thrombin-binding substances have the following characteristics:

Thrombin-binding protein substance and process for preparing the same

A monoclonal antibody which is specific to human protein C which has calcium bound at the gammacarboxyglutamic acid(Gla) domain and does not recognize human protein C which is not bound to calcium at the Gla domain. The monoclonal antibody is used in an immunoassay method for determining human protein C having a Gla domain and in a method for recovering human protein C having a Gal domain.

Monoclonal antibody to human protein C

A novel thrombin-binding substance having the characteristics of (a) molecular weight: 47,000.+-.6,000 in reduced condition and 38,000.+-.6,000 in unreduced condition, (b) isoelectric point: pH 4.9-5.7, (c) affinity: strong affinity to thrombin, (d) activity: (1) capable of promoting the thrombin catalyzed activation of protein C, (2) prolongs clotting time; and (e) stability: stable to denaturing agents (urea sodium and dodecylsulfate), can be prepared from a human placenta by means of extraction, fractionation using ion exchange chromatography and affinity chromatography, and/or gel filtration, followed by electrophoresis. The substance is useful as a medicine for the treatment of thrombosis.

Thrombin-binding substance and process for preparing the same

A thrombin-binding substance derived from human tissue and having the characteristics of (a) molecular weight: 88,000.+-.20,000 in reduced condition and 71,000.+-.20,000 in unreduced condition; (b) isoelectric point: .sub.p H 4.2.+-.0.5; (c) affinity: strong for thrombin; (d) activities: capable of promoting the thrombin-catalyzed activation of protein C and prolonging clotting time; and (e) stability: stable over a .sub.p H range of 2 to 10 and stable to denaturing agents (sodium dodecylsulfate and urea) and to a pepsin treatment, is effectively useful for thrombolysis and anticoagulation.

Thrombin-binding substance and process for its production

A peptide of the formula: ##STR1## wherein G-COOH is Glu, and R is an amino or chromophore group is effective as a therapeutic drug for hemostatic disorders and thrombosis.

Peptides

Compound of the formula, ##STR1## wherein X is a hydrogen atom, a halogen atom, a lower alkyl group or a lower alkoxyl group, R.sup.1 is a methyl group or an ethyl group, R.sup.2 is a hydrogen atom, a lower alkyl group or an allyl group, and each of R.sup.3 and R.sup.4, independently, is a hydrogen atom, a methyl group or an ethyl group; provided that R.sup.1, R.sup.3 and R.sup.4 are not methyl groups simultaneously when both X and R.sup.2 are hydrogen atoms, and compositions containing these compounds exhibit herbicidal activity.

Urea compounds and herbicidal compositions containing them

Growing community of inventors

Tokyo, Japan

Nobuo Aoki