Seikagaku Corporation

Seikagaku Kogyo Kabushiki Kaisha (seikagaku Corporation)

Nec Corporation

National Institute of Advanced Industrial Science and Technology

Seikagaku Kogyo Kabushiki Kaisha

Seikgaka Corporation

Hideo Mochizuki

Nobukazu Hashimoto

Akio Hamai

Hisashi Narimatsu

Shigemi Sugioka

Kiyoshi Suzuki

Satoshi Miyauchi

Masami Iida

Akira Tawada

Yeong Shik Kim

Junichi Onaya

Yuji Matsuzaki

Yousuke Yasuda

Yusuke Hori

Kiwamu Yamagishi

To provide a polypeptide having heparosan-glucuronate 5-epimerase activity, whereby means for producing a polysaccharide in which hexuronic acid residues has been epimerized is provided. Through screening ofcDNA library, a DNA encoding a polypeptide of heparosan-glucuronate 5-epimerase is obtained. The epimerase acts on glucuronic acid residues of N-acetyl heparosan and/or iduronic acid residues of completely desulfated N-acetylated heparin. The polypeptide encoded by the DNA is expressed by insect cells, to thereby yield the polypeptide having heparosan-glucuronate 5-epimerase activity. By bringing the polypeptide into contact with N-acetyl heparosan or completely desulfated N-acetylated heparin, a polysaccharide in which hexuronic acid residues has been epimerized is yielded.

Heparosan-glucuronic acid-5-epimerase, and method for producing polysaccharide using same

A glycosaminoglycan sulfotransferase, a peptide thereof, a nucleic acid comprising a nucleotide sequence encoding the same, an enzyme agent for the synthesis of a glycosaminoglycan, which comprises the above-described enzyme or polypeptide, and a process for producing a glycosaminoglycan, which uses the enzyme agent.

Sulfotransferase, peptide thereof and DNA encoding the same

Sulfotransferase, its polypeptide and DNA encoding the same

Method for producing oligosaccharide, and novel oligosaccharide and pharmaceutical composition containing the same

A crystallizable, purified chondroitinase ABC having a molecular weight of about 100,000 dalton by the measurement of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and the measurement by the gel permeation chromatography method, having alanine as the N-terminal amino acid and proline as the C-terminal amino acid. A process for the purification of the crystallizable purified chondroitinase ABC comprising removing nucleic acid from an surfactant solution extract obtained from cells of chondroitinase ABC-producing microorganisms and chromatographically treating by concentration gradient elution using a weak cation exchange resin or a strong cation exchange resin. A composition comprising a chondroitinase and serum albumin, gelatin, or a nonionic surfactant.

Chondroitinase, process for preparing the same, and pharmaceutical composition comprising the same

The processor comprises a storage unit for accommodating data required for operations and operation results and an arithmetic unit for processing an operation using operation data read from the storage unit, and incorporates a operation command group for being executed by the arithmetic unit, generating an operation result having a bit width greater than the bit width of the storage unit and accommodating a part of the data of the operation result having a bit width less than the bit width of the storage unit and required for a subsequent operation in said operation data storing means as data to be accommodated in the storage unit.

Processor and its operation processing method for processing operation

A crystallizable, purified chondroitinase ABC having a molecular weight of about 100,000 dalton by the measurement of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and the measurement by the gel permeation chromatography method, having alanine as the N-terminal amino acid and proline as the C-terminal amino acid is disclosed. A process for the purification of the crystallizable purified chondroitinase ABC comprising removing nucleic acid from an surfactant solution extract obtained from cells of chondroitinase ABC-producing microorganisms and chromatographically treating by concentration gradient elution using a weak cation exchange resin or a strong cation exchange resin is disclosed. A composition comprising a chondroitinase and serum albumin, gelatin, or a nonionic surfactant is disclosed. The enzyme is isolated from Proteus vulgaris ATCC 6896.

Crystalline chondroitinase isolated from Proteus vulgaris ATCC 6896

Producing pure chondroitinase ABC from Proteus vulgaris ATCC 6896

A crystallizable, purified chondroitinase ABC having a molecular weight of about 100,000 dalton by the measurement of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and the measurement by the gel permeation chromatography method, having alanine as the N-terminal amino acid and proline as the C-terminal amino acid. A process for the purification of the crystallizable purified chondroitinase ABC comprising removing nucleic acid from an surfactant solution extract obtained from cells of chondroitinase ABC-producing microorganisms and chromatographically treating by concentration gradient elution using a weak cation exchange resin or a strong cation exchange resin. A composition comprising a chondroitinase and serum albumin, gelatin, or a nonionic surfactant. The chondroitinase ABC is isolated from Proteus vulgaris ATCC 6896.

Chondroitinase ABC isolated from proteus vulgaris ATCC 6896

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Nagoya, Japan

Hideo Mochizuki