Other

Kabushikikaisha Kibun Foodchemifa

Chichibu Cement Co., Ltd.

Kabushikikaisha Kibun

Tokiwa Chemical Industries Co., Ltd.

Kabushiki Kaisha Kibun Shokuhin

Tokiwa Chemical Industries, Limited

Chichibu Onoda Cement Corp.

Protein Express Co., Ltd.

Yuichi Ishida

Takeda Chem. Ind. Ltd.

Kabushikikiaisha Kibun Foodchemifa

Kabushikikiaisha Kibun

Kazuo Murakami

Fumiaki Suzuki

Katsumi Murata

Isao Kusakabe

Yukio Nakamura

Naoto Ueno

Yukio Kato

Hiroshi Kiuchi

Hideyuki Kobayashi

Yasuhiko Hatano

Toshihide Satoh

There are provided a method for selection of a substance which is capable of controlling activation of prorenin where an adjusting ability of the activation of prorenin by protein-protein interaction in a profragment region of prorenin as indicator is used; a prorenin activation controlling substance having a function of controlling the activation of prorenin based on protein-protein interaction by a profragment region of prorenin; and hypotensor, organ hypertrophy suppressor and arterial thickening suppressor containing the prorenin activation controlling substance as an effective ingredient.

Hypotensors

Disclosed is a novel renin-active substance by utilizing a anti-peptide antibody capable of specifically recognizing a specific amino acid sequence in the human propenin profragment exemplified, as a typical example, by a complex formed from human prorenin and an anti-peptide antibody capable of specifically recognizing an amino acid sequence consisting of at least 15 amino acid residues located within an amino acid sequence consisting of 33 amino acid residues between the isoleucine residue at the 11th site and the arginine residue at the 43rd site within human propenin profragment having an amino acid sequence consisting of 43 amino acid residues.

Renin-active substance

Provided by the present invention are a human prorenin profragment N-terminated peptide antibody capable of specifically recognizing a peptide containing at least 15 amino acid residues from the first leucine residue to the 15th arginine residue in the N-terminated peptide of the human prorenin profragment and a complex of the same with human prorenin. The antibody can be used as a prorenin assay reagent. The human prorenin profragment N-terminated peptide antibody is useful as a reagent for the assay of human prorenin in blood.

Prorenin antibody and renin-active substance containing the same

Disclosed are (1) a Xenopus laevis bone morphogenetic protein (BMP), (2) a DNA comprising a DNA segment coding for a Xenopus laevis BMP, (3) a transformant bearing a DNA comprising a DNA segment coding for a Xenopus laevis BMP and (4) a method for preparing the Xenopus laevis BMP which comprises culturing the described in (3), producing and accumulating the protein in a culture, and collecting the protein thus obtained. Cells transinfected or transformed with the DNA allow large amounts of the Xenopus laevis BMP mature peptides to be produced, which causes the advantageous production of the peptides, which promote the synthesis of proteoglycan and can also be utilized for analysis of the mechanism of organism, particularly human bone-cartilage morphogenetic reaction, and as therapeutic agents for osteoporosis.

DNA encoding bone morphogenetic proteins, host cells transformed there

Disclosed are (1) a Xenopus laevis bone morphogenetic protein (BMP), (2) a DNA comprising a DNA segment coding for a Xenopus laevis BMP, (3) a transformant bearing a DNA comprising a DNA segment coding for a Xenopus laevis BMP and (4) a method for preparing the Xenopus laevis BMP which comprises culturing the described in (3), producing and accumulating the protein in a culture, and collecting the protein thus obtained. Cells transfected or transformed with the DNA allow large amounts of the Xenopus laevis BMP mature peptides to be produced, which causes the advantageous production of the peptides, which promote the synthesis of proteoglycan and can also be utilized for analysis of the mechanism of organism, particularly human bone-cartilage morphogenetic reaction, and as therapeutic agents for osteoporosis.

Xenopus laevis bone morphogenetic proteins and use thereof

The present invention relates to alginase produced by bacteria belonging to the genus and a process for production thereof and bacteria as well as a method for decomposing alginic acid.

Production of alginase from Enterobacter cloacae M-1 (FERM BP-2577)

Protein obtained by coagulating soymilk with microbially produced protease within a pH range not causing acid coagulation and at a temperature higher than the optimum operation temperature of the protease provides food material of desirable flavor and high processability.

Process for producing food material

Soybean milk is treated with protease at a pH in the range which does not cause acid coagulation in the presence of a magnesium salt as a concentration in the range which does not substantially cause magnesium coagulation, to flocculate protein in soybean milk, thereby a food material having good mouthfeel and high processability may be obtained.

Process for the production of a food material

Growing community of inventors

Tsukuba, Japan

Kazuo Murakami