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90 results on '"Takahara, Yoshiyuki"'

3. The hypocholesterolemic effects of Cistanche tubulosa extract, a Chinese traditional crude medicine, in mice

Author

Shimoda, Hiroshi, Tanaka, Junji, Takahara, Yoshiyuki, Takemoto, Kazuhisa, Shan, Shao-Jie, and Su, Muh-Hwan

Subjects
Hypocholesteremia -- Development and progression, Hypocholesteremia -- Research, Lamiales -- Chemical properties, Lamiales -- Health aspects, Lamiales -- Research, Medicine, Chinese -- Research, Cholesterol, LDL -- Research, Cholesterol metabolism -- Research, Health
Published
2009

6. Identification and cloning of an Erwina carotovora subsp. carotovora bacteriocin regulator gene by insertional mutagenesis

Author

Chuang, Duen-Yau, Kyeremeh, Ampaabeng G., Gunji, Yuichi, Takahara, Yoshiyuki, Ehara, Yoshio, and Kikumoto, Toshio

Subjects
Bacteria, Phytopathogenic -- Genetic aspects, Bacterial toxins -- Genetic aspects, Biological sciences
Abstract

DNA containing the bacteriocin regulator gene (brg) from the phytopathogenic bacterium Erwinia carotovora subsp. carotovora CGE234M403's rifampin-resistant mutant, M-rif-11-2 were cloned and sequenced. One complete open reading frame (ORF), called ORF2, was found within the sequenced fragment. The 3' end of another ORF, ORF1, was found upstream of ORF2. A noncoding region and a putative promoter were found between ORF1 and ORF2.

Published
1999

29. Nucleotide Sequences and Organization of the Genes for Carotovoricin (Ctv) from Erwinia carotovora Indicate That Ctv Evolved from the Same Ancestor as Salmonella typhi Prophage.

Author

Yamada, Kazuteru, Hirota, Morihiko, Niimi, Yoshiko, Nguyen, Hoa Anh, Takahara, Yoshiyuki, Kami, Yoshiyuki, and Kaneko, Jun

Subjects
ERWINIA carotovora, GENES, BACTERIOPHAGES, NUCLEOTIDE sequence, BIOCHEMISTRY, BIOTECHNOLOGY
Abstract

The article focuses on the study conducted in Japan regarding the evolution of nucleotide sequences and organization of genes for Carotovocin from Erwinia carotovora. The authors discuss the gene organization and deduced amino acid sequences of carotovoricins in the chromosome on Salmonella enterica. Moreover, they talk about the mosaic structure of CtvEr genes and Mu-like prophage genes.

Published
2006
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32. Nucleotide Sequences and Organization of the Genes for Carotovoricin (Ctv) from Erwinia carotovoraIndicate That Ctv Evolved from the Same Ancestor as Salmonella typhiProphage

Author

YAMADA, Kazuteru, HIROTA, Morihiko, NIIMI, Yoshiko, NGUYEN, Hoa Anh, TAKAHARA, Yoshiyuki, KAMIO, Yoshiyuki, and KANEKO, Jun

Abstract

Carotovoricin Er (CtvEr), which is produced by a plant soft rot disease causative agent, Erwinia carotovorasubsp. carotovoraEr, is a high-molecular-weight bacteriocin showing Myoviridae phage-tail-like morphology with contractile sheath and plural tail fibers. We determined the complete nucleotide sequences of CtvEr genes on the E. carotovoraEr chromosome and report that CtvEr genes consist of lysis cassette, major and minor structural protein gene clusters. Four promoters were identified. The lysis gene cassette, which is composed of the genes for lysis enzyme and holin, was also identified and characterized. The nucleotide sequences and organization of the genes for CtvCGE, which is produced by E. carotovorastrain CGE234-M403 with the morphology similar to CtvEr, were also determined and compared to that of CtvEr, and it was found that CtvCGE is almost identical to CtvEr except for tail fibers which are involved in the killing spectra of both bacteriocins. We also explain that the gene organization and the deduced amino acid sequences of both carotovoricins are very close to those of prophage, which is lysogenized in the chromosome on Salmonella entericaserovar Typhi CT18. These findings strongly suggest that Ctv evolved as a phage tail-like bacteriocin from a common ancestor with Salmonella typhiprophage.

Published
2006
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33. High yield refolding and purification process for recombinant human interleukin-6 expressed in <TOGGLE>Escherichia coli</TOGGLE>

Author

Ejima, Daisuke, Watanabe, Mayumi, Sato, Yutaka, Date, Masayo, Yamada, Naoyuki, and Takahara, Yoshiyuki

Abstract

Recombinant human interleukin-6 (hIL-6), a pleiotropic cytokine containing two intramolecular disulfide bonds, was expressed in Escherichia coli as an insoluble inclusion body, before being refolded and purified in high yield providing sufficient qualities for clinical use. Quantitative reconstitution of the native disulfide bonds of hIL-6 from the fully denatured E. coli extracts could be performed by glutathione-assisted oxidation in a completely denaturating condition (6M guanidinium chloride) at protein concentrations higher than 1 mg/mL, preventing aggregation of reduced hIL-6. Oxidation in 6M guanidinium chloride (GdnHCl) required remarkably low concentrations of glutathione (reduced form, 0.01 mM; oxidized form, 0.002 mM) to be added to the solubilized hIL-6 before the incubation at pH 8.5, and 22°C for 16 h. After completion of refolding by rapid transfer of oxidized hIL-6 into acetate buffer by gel filtration chromatography, residual contaminants including endotoxin and E. coli proteins were efficiently removed by successive steps of chromatography. The amount of dimeric hIL-6s, thought to be purification artifacts, was decreased by optimizing the salt concentrations of the loading materials in the ion-exchange chromatography, and gradually removing organic solvents from the collected fractions of the preparative reverse-phase HPLC. These refolding and purification processes, which give an overall yield as high as 17%, seem to be appropriate for the commercial scale production of hIL-6 for therapeutic use. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 62: 301–310, 1999.

Published
1999
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34. Studies of Sulfonyl Radicals. II. Relative Reactivities of Addition Reactions of Sulfonyl Free Radicals to Vinyl Monomers

Author

Takahara, Yoshiyuki, Iino, Masashi, and Matsuda, Minoru

Abstract

Addition reactions of various vinyl monomers towards the free methanesulfonyl and arenesulfonyl radicals have been investigated. Relative reactivities of p-methylstyrene (M2) to styrene (M1) towards methane- and para-substituted benzenesulfonyl radicals are hardly affected by the kind of sulfonyl radical, suggesting that an unpaired electron of methanesulfonyl and arenesulfonyl radicals is localized mainly on sulfonyl groups. Relative reactivities obtained with vinyl monomers were correlated to Hammett’s spvalues with ?p=-3.6 and also to Alfrey-Price’s evalues, indicating that sulfonyl radicals are strongly electrophilic. The highest selectivity of the benzenesulfonyl radical, obtained in the comparison of the selectivity of a number of radicals in addition reactions towards three representative monomers (Table 5), also supports the above conclusion.

Published
1976
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35. Purification of enzymatically active poliovirus proteinase 3C produced in Escherichia coli

Author

Kondo Kiyosi, Kohara Michinori, Takahara Yoshiyuki, Hagino-Yamagishi Kimiko, Itoh Heihachi, Nomoto Akio, Ando Noriko, and Numao Naganori

Subjects
Viral protein, medicine.drug_class, viruses, Immunoblotting, Biology, medicine.disease_cause, Monoclonal antibody, law.invention, Viral Proteins, Capsid, Transformation, Genetic, law, Genetics, medicine, Escherichia coli, Cloning, Molecular, Protein Precursors, Gel electrophoresis, Chromatography, Poliovirus, Viral protein processing, 3C Viral Proteases, virus diseases, General Medicine, biochemical phenomena, metabolism, and nutrition, Molecular biology, Cysteine Endopeptidases, DNA, Viral, Recombinant DNA, Electrophoresis, Polyacrylamide Gel, Protein Processing, Post-Translational, Plasmids
Abstract

A viral protein 3C of the poliovirus (PV) Sabin 2 strain, a possible core region of the viral proteinase, was expressed in Escherichia coli using a recombinant DNA technology. The protein was recovered as a soluble protein from the insoluble protein fraction of the bacterial lysate, and was purified by a simple procedure with column chromatography. The viral capsid precursor P1 (1ABCD) of the PV Sabin 3 strain, which had been similarly produced in E. coli, was mixed with the purified or crude recombinant 3C. Immunoblotting assay with monoclonal antibodies specific to capsid proteins 1C (VP3) and 1D (VP1) of the PV Sabin 3 strain revealed that the in vitro reaction products contained 1C (VP3), 1D (VP1) and 1ABC (VP0–VP3). The data indicated that processing of the polyprotein P l by the recombinant 3C proceeded properly in vitro, although an undigested product, 1ABC, is always detected in the reaction mixture. The results strongly suggest that, in addition to a protein 3CD, the 3C protein itself is also catalytically active in the processing of the viral capsid precursor polyprotein P1.

Published
1989

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