31 results on '"Yoshio Takizawa"'
Search Results
2. Suggestions for maintenance checks of the Rope-net method
- Author
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Shinichi Arai, Ryuta Suzaki, Masaya Fujita, Atsushi Yashima, Yoshio Takizawa, and Kazuhide Sawada
- Subjects
Rope ,Mathematics ,Marine engineering - Abstract
斜面に存在する岩塊を安定化させるために用いられるロープネット工に関する維持管理の課題を解決するため,現地調査,素線のめっき量調査および腐食ロープの引張試験を実施した。現地調査の結果,ロープネット工には,さびによる腐食が発生しやすく,それらはワイヤーロープが立木や地表面に接している箇所に発生しやすいことがわかった。素線のめっき量調査結果から,良好な山林環境におけるワイヤーロープ部材の耐用年数は100年以上期待できることがわかった。また,腐食ロープの引張試験結果から,ワイヤーロープの寿命曲線を提案し,腐食しやすい箇所は施工後20年程度でワイヤーロープの部材を交換しなければならないことがわかった。以上のことからロープネット工施設は,適切な維持管理により腐食部材を順次交換することにより,30年程度と考えられていた施設の耐用年数を大幅に延ばすことが可能である。
- Published
- 2010
3. Efficient routine investigation method for maintenance of prevention structure against falling rock using GPS information
- Author
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Yoshio Takizawa, Kazuhide Sawada, Ryuta Suzaki, Shinichi Arai, Masaya Fujita, and Atsushi Yashima
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Investigation methods ,business.industry ,Computer science ,Gps global positioning system ,Global Positioning System ,business ,Geodesy ,Remote sensing - Abstract
本論文は,携帯GPS装置を用いた落石予防施設の模擬点検結果から,落石予防施設の効率的な維持点検手法を提案するものである。模擬点検は,全10箇所のロープネット工施設を対象に実施し,施設の位置情報として地形図のみを与えたA班と,地形図に加えGPS座標情報を与えたB班の2班を用意し,現場到達時間を比較した。この結果,B班の合計時間がA班と比較して42%短くなり,GPS座標情報によって維持点検作業を効率的に実施可能であることがわかった。施設の位置情報としてGPS座標情報等を盛り込んだGISを構築することにより,点検データの一元管理,最新の地形図利用,アクセスルート等の情報共有が可能となる。また,今後の点検計画の立案が容易になるなど施設の維持管理を効率的に行うことが可能となる。
- Published
- 2009
4. The Corrosion Behavior of Ni-Cr-Mo Ternary Alloys in Hot Concentrated Sulfuric Acids with Active Carbon (Part 3)
- Author
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Katsuo Sugahara and Yoshio Takizawa
- Subjects
Active carbon ,Materials science ,Inorganic chemistry ,Metals and Alloys ,Tantalum ,chemistry.chemical_element ,Sulfuric acid ,Surfaces, Coatings and Films ,chemistry.chemical_compound ,chemistry ,X-ray photoelectron spectroscopy ,Materials Chemistry ,Electrochemistry ,Ternary operation ,Corrosion behavior - Published
- 1998
5. The Corrosion Behavior of Ni-Cr-Mo Ternary Alloys in Hot Concentrated Sulfuric Acids with Active Carbon (Part 1)
- Author
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Katsuo Sugahara, Eiji Akiyama, Yoshio Takizawa, and Koji Hashimoto
- Subjects
Active carbon ,chemistry.chemical_compound ,Materials science ,chemistry ,X-ray photoelectron spectroscopy ,Inorganic chemistry ,Materials Chemistry ,Electrochemistry ,Metals and Alloys ,Sulfuric acid ,Ternary operation ,Corrosion behavior ,Surfaces, Coatings and Films - Published
- 1997
6. Corrosion-resistant NiCrMo alloys in hot concentrated sulphuric acid with active carbon
- Author
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Yoshio Takizawa and Katsuo Sugahara
- Subjects
inorganic chemicals ,Active carbon ,Materials science ,Mechanical Engineering ,Metallurgy ,Alloy ,technology, industry, and agriculture ,chemistry.chemical_element ,engineering.material ,equipment and supplies ,Condensed Matter Physics ,Corrosion ,Cathodic protection ,Chromium ,chemistry ,Mechanics of Materials ,Molybdenum ,engineering ,General Materials Science ,Ternary operation ,Dissolution - Abstract
Dewpoint corrosion by sulphuric acid has often been observed in the heat exchangers of coal-burning plants. If ashes contain active carbon, corrosion becomes particularly serious. Various nickel-base alloys with high corrosion resistance in such environments have been designed. The corrosion behaviour of these alloys was examined in hot concentrated sulphuric acid with and without active carbon. The corrosion resistance of ternary NiCiMo alloys in the acids without active carbon increases with increasing alloy molybdenum content. When active carbon is added to the acids, the corrosion rate increases significantly. This is due to acceleration of transpassive dissolution of molybdenum as a result of enhancement of cathodic activity with the addition of active carbon. The corrosion resistance in the acids with active carbon is enhanced by an increase in alloy chromium content, which improves the passivity in the acids.
- Published
- 1995
7. MAT^|^reg;21PAT, Corrosion Resistant Nickel-based Alloy
- Author
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Yoshio Takizawa and Katsuo Sugahara
- Subjects
6111 aluminium alloy ,Materials science ,Metallurgy ,Alloy ,Metals and Alloys ,Nickel based ,5005 aluminium alloy ,engineering.material ,Surfaces, Coatings and Films ,Corrosion resistant ,Materials Chemistry ,Electrochemistry ,5052 aluminium alloy ,engineering ,6063 aluminium alloy - Published
- 2000
8. Fundamental Study on the Corrosion Mechanism of Zr-0.2Fe, Zr-0.2Cr, and Zr-0.1Fe-0.1Cr Alloys
- Author
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Takuya Murai, Yoshio Takizawa, Takeshi Isobe, and Mae Yoshiharu
- Subjects
6111 aluminium alloy ,Fundamental study ,Materials science ,Zirconium alloy ,Metallurgy ,Electrochemistry ,Anodic protection ,Corrosion - Published
- 2008
9. Primary Structure of an Alkaline Ribonuclease from Bovine Liver1
- Author
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Hideaki Watanabe, Yoshio Takizawa, Kazuko Ohgi, Shuichi Hasemi, Masachika Irie, Kenji Hosoya, Akihiro Sanda, and Yasuo Nagareda
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chemistry.chemical_classification ,Gel electrophoresis ,Edman degradation ,medicine.diagnostic_test ,RNase P ,Proteolysis ,Protein primary structure ,General Medicine ,Biochemistry ,Homology (biology) ,Amino acid ,Enzyme ,chemistry ,medicine ,Molecular Biology - Abstract
A pyrimidine base specific and most basic alkaline RNase named RNase BL4 was isolated from bovine liver as a protein showing a single band on slab gel-electrophoresis. The enzyme is most active at pH 7.5. The enzyme was immunologically distinguishable from the known bovine RNases such as pancreatic RNase (RNase A), seminal RNase, kidney non-secretory RNase (RNase K2), and brain RNase (RNase BRb). The primary structure of this pyrimidine base-specific RNase was determined to be less than EDRMYQRFLRQHVDPDETG- GNDSYCNLMMQRRKMTSHQCKRFNTFIHEDLWNIRSICSTTNIQCKNGQMNCHEGVVRV- TDCRETGSSRAPNCRYRAKASTRRVVIACEGNPEVPVHFDK. It consists of 119 amino acid residues, and is 5 amino acid residues shorter than RNase A. The sequence homology of RNase BL4 with RNase A is 46.2%, and optimal alignment of RNase A and RNase BL4 requires five deletions, one at the 24th position, two at the 75th and 76th positions, and two at the C-terminus in RNase BL4. The RNase BL4 was highly homologous with a porcine liver RNase (RNase PL3, 94.1% homology) studied by Hofsteenge et al. (personal communication from Hofsteenge, J., Matthies, R., and Stones, S.R.).
- Published
- 1990
10. Two-generation reproduction toxicity study in rats with 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane (p,p'-DDT)
- Author
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Masayuki Araki, Machiko Saka, Shoji Teramoto, Maki Kuwahara, Hitoshi Hojo, Hiroaki Aoyama, Ken L. Takahashi, Koji Sakasai, Yoshio Takizawa, and N. Shimizu
- Subjects
Two generation ,Male ,Embryology ,medicine.medical_specialty ,media_common.quotation_subject ,Endogeny ,Biology ,DDT ,Rats, Sprague-Dawley ,Pregnancy ,Internal medicine ,medicine ,Endocrine system ,Sexual maturity ,Animals ,Pesticides ,Progesterone ,media_common ,Dose-Response Relationship, Drug ,Estradiol ,Body Weight ,Abnormalities, Drug-Induced ,Estrogens ,General Medicine ,Pesticide ,Rats ,Endocrinology ,Liver ,Pediatrics, Perinatology and Child Health ,Toxicity ,Pregnancy, Animal ,Female ,Reproduction ,Reproductive toxicity ,Developmental Biology - Abstract
DDT, an organochlorine pesticide, has been cited as a representative chemical suspected of having endocrine disrupting effects. In this study, the potential endocrine disrupting activities of p,p'-DDT, a major component of DDT, were investigated in rats in a 2-generation reproduction toxicity study in accordance with the most current test guidelines of the Ministry of Agriculture, Forestry and Fisheries in Japan, Organization for Economic Cooperation and Development (OECD) and United States Environmental Protection Agency (USEPA) with some modifications and additions. p,p'-DDT was given to parental rats at dietary levels of 0, 5, 50 or 350 ppm. Systemic toxicities in the parental animals consisted of tremors and subsequent deaths (females only) and/or pathological alterations of the liver (both sexes of animals) of the 2 higher dose groups. Reproductive and postnatal developmental toxicities were not evident up to the highest dose level except for the decreased pup viability index on postnatal day 21 in the 350 ppm group. Changes in serum estradiol and progesterone levels and/or a delay in male sexual maturation were noted in the 2 higher dose groups in a dose-dependent fashion, suggesting alterations of endogenous endocrine functions. However, these changes never resulted in substantial reproductive disorders.
- Published
- 2006
11. Lens luxation in a CD-1 mouse
- Author
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Koji Sakasai, Yoshio Takizawa, Koichi Y. Ebino, and Takanori Harada
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Male ,genetic structures ,Eye Diseases ,Lens luxation ,Conical cornea ,Adhesion (medicine) ,General Biochemistry, Genetics and Molecular Biology ,Cornea ,Rodent Diseases ,Mice ,Lens, Crystalline ,medicine ,Animals ,Iris (anatomy) ,Synechia ,Mice, Inbred ICR ,General Veterinary ,Neovascularization, Pathologic ,business.industry ,General Medicine ,Anatomy ,Lens Subluxation ,medicine.disease ,eye diseases ,Ophthalmoscopy ,medicine.anatomical_structure ,Lens (anatomy) ,Corneal neovascularization ,Animal Science and Zoology ,sense organs ,business - Abstract
Lens luxation was found in a male CD-1 (ICR) mouse. Ophthalmologic examinations revealed conical cornea anterior synechia and corneal neovascularization in the right eye. The lens was dislocated heterocentrically within the posterior chamber. Histologically, anterior lens luxation and adhesion between the iris and cornea were observed.
- Published
- 1996
12. 4826578 Method of producing heat-transfer material
- Author
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Naokazu Yoshiki, Takahashi Tsutomu, Yoshio Takizawa, and Yasuo Masuda
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General Energy ,Materials science ,Heat transfer ,General Engineering ,Composite material - Published
- 1990
13. Carboxymethylation of a ribonuclease from Rhizopus sp
- Author
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Yoshio Takizawa, Masachika Irie, and Akihiro Sanda
- Subjects
chemistry.chemical_classification ,biology ,Stereochemistry ,RNase P ,Active site ,General Chemistry ,General Medicine ,biology.organism_classification ,RNase PH ,Residue (chemistry) ,Enzyme ,Biochemistry ,chemistry ,Rhizopus ,Drug Discovery ,biology.protein ,Ribonuclease ,Histidine - Abstract
In order to investigate the nature of the amino acid residues involved in the active site of a ribonuclease from Rhizopus sp. (RNase Rh), carboxymethylation of RNase Rh with iodoacetate was performed. RNase Rh was found to be inactivated markedly at pH 3-5 by iodoacetate. From the pH profile of the rate of inactivation of RNase Rh, it was suggested that functional groups having pKa values of ca. 7.3 and 4.3 might be involved in this inactivation reaction. The determination of the amino acid composition of RNase Rh inactivated by iodoacetate at pH 5.0 indicated that the formation of about one residue of N3-carboxymethylhistidine was responsible for the loss of enzymatic activity. The results were very similar to those for an RNase from Asp. saitoi having very similar base specificity. The carboxymethylation of RNase Rh was inhibited by competitive inhibitors. Thus, the histidine residue modified might be involved in the active site of the enzyme.
- Published
- 1985
14. Primary Structure of a Ribonuclease from Bovine Brain1
- Author
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Katoh H, Ishii M, Komoda Y, Kazuko Ohgi, Yoshio Takizawa, Masachika Irie, Akihiro Sanda, and Hideaki Watanabe
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chemistry.chemical_classification ,Arginine ,RNase P ,Protein primary structure ,General Medicine ,Biology ,Biochemistry ,Amino acid ,Serine ,chemistry ,biology.protein ,Proline ,Ribonuclease ,Molecular Biology ,Histidine - Abstract
The primary structure of a pyrimidine base-specific ribonuclease from bovine brain was determined. The sequence determined is (sequence; see text). Although the sequence homology of this RNase with bovine pancreatic RNase A is 78.2%, it consists of 140 amino acid residues, and it is 16 amino acid residues longer than RNase A at the carboxyl-terminal. In addition to an N-glycosylated long carbohydrate chain, the bovine brain RNase has two short O-glycosylated carbohydrate chains at the 129th and the 133rd serine residues. The additional C-terminal tail of the bovine brain RNase has a unique composition: 6 proline, 5 hydrophobic amino acids, and two basic amino acids, arginine and histidine.
- Published
- 1988
15. Case Studies on Pitting Corrosion Failures of Copper Tubes in Hot Water
- Author
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Yoshihiro Hisamatsu, Yoshio Takizawa, Saburo Okada, Ichiro Suzuki, Hiroshi Yamamoto, Kiichi Nawata, Haruo Baba, Shigenori Yamauchi, Shiro Sato, Tetsuo Fujii, Kuniaki Seki, Tateki Minamoto, and Toshiaki Kodama
- Subjects
Materials science ,chemistry ,Metallurgy ,General Engineering ,Pitting corrosion ,chemistry.chemical_element ,General Materials Science ,Erosion corrosion of copper water tubes ,Copper - Published
- 1982
16. Distribution of a kidney acid-ribonuclease-like enzyme and the other ribonucleases in bovine organs and body fluids
- Author
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Kazuko Ohgi, Masachika Irie, Torn Morita, Akihiro Sanda, and Yoshio Takizawa
- Subjects
chemistry.chemical_classification ,biology ,medicine.diagnostic_test ,Chemistry ,RNase P ,Molecular biology ,RNase PH ,General Biochemistry, Genetics and Molecular Biology ,Enzyme assay ,Enzyme ,Biochemistry ,Immunoassay ,biology.protein ,medicine ,Ribonuclease ,General Agricultural and Biological Sciences ,RNase H ,Gene - Abstract
To determine the distribution of a kidney acid RNase (RNase K2) and other RNases, the levels of RNase K2, RNase A, and seminal RNase (RNase Vs1) in bovine tissues and body fluids were measured by enzyme immunoassay. The crude extracts of several tissues and body fluids were fractionated by phospho-cellulose column chromatography. The enzymatic activities at pH 7.5 and 6.0 and enzyme contents of each tube were measured by enzyme assay and enzyme immunoassay, respectively. In the pancreas, parotid gland, and heart, most RNase activity was due to a single peak of RNase A, but a small amount of RNase K2 was always observed. In the kidney, there was about 5 times as much RNase K2 as RNase A. In the lung, although RNase K2 and RNase A were the major components, there are another two alkaline RNase peaks. In the spleen and liver, there are four RNases, two acid RNases, one of which is RNase K2, and two alkaline RNases including RNase A. A new acid RNase (non RNase K2-acid RNase) from both organs was immunologically the same. In serum, there are at least four RNases. By partial purification of serum RNases by phosphocellulose and heparin-Sepharose column chromatographies, at least 4 RNases, RNase A, RNase K2 and the other two alkaline RNases, one of which is immunologically indistinguishable from liver alkaline RNase, were confirmed. The other serum alkaline RNase was immunologically related to lung and spleen alkaline RNases. In conclusion, in bovine tissues and body fluids there are at least 7 types of pyrimidine-base-specific RNases: brain RNase, seminal RNase, RNase A, RNase K2, an acid RNase (RNase BSP1), an alkaline RNase (RNase BL4), and another alkaline RNase in serum.
- Published
- 1987
17. Thermoswitching property in TCNQ salts of ionenes containing poly(ethylene oxide) segments
- Author
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Isao Shinohara, Masayoshi Watanabe, Yoshio Takizawa, and Hirotsugu Aiga
- Subjects
Arrhenius equation ,chemistry.chemical_classification ,Materials science ,Ethylene oxide ,Transition temperature ,Oxide ,Polymer ,Microstructure ,chemistry.chemical_compound ,symbols.namesake ,Crystallography ,chemistry ,Electrical resistivity and conductivity ,Polymer chemistry ,symbols ,Melting point - Abstract
Ionene polymers characterized by the alternating structure of ionene and crystalline poly(ethylene oxide) (PEO) segments were prepared as a function of PEO segment size. A microstructure of these ionenes and their 7,7,8,8-tetracyanoquinodimethane (TCNQ) salts were investigated with x-ray diffraction patterns, thermal scanning behavior, and polarizing micrographs. On the basis of this microstructure, the change in resistivity with temperature was studied. In Arrhenius' plots of the resistivity the simple salts in which the spherulites consisting of the PEO segments were observed showed a sharp decrease in resistivity with a rise in temperature [critical temperature resistor (CTR)] at about the melting point of the PEO segments, whereas the other simple salts in which the spherulites were not observed showed linear temperature dependence. The switching properties were confirmed similarly in repetitive heating/cooling cycles. This CTR characteristic was attributed to an increase in continuity in the conduction paths by melting spherulites. The apparent switching properties were not observed in the complex salts.
- Published
- 1983
18. Microstructure and electric properties of elastomeric ionene-TCNQ salts
- Author
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Yoshio Takizawa, Nobuhiro Toneaki, Masayoshi Watanabe, and Isao Shinohara
- Subjects
chemistry.chemical_classification ,Materials science ,chemistry ,Electrical resistivity and conductivity ,Polymer chemistry ,Analytical chemistry ,Molecule ,Polymer ,Activation energy ,Dielectric ,Microstructure ,Elastomer ,Polarization (electrochemistry) - Abstract
The elastomeric ionene polymers characterized by the alternating structure of the rigid polycation segments that contained 4,4′-bipyridilium rings and the flexible polypropyleneoxide (PPO) segments were prepared as a function of chain length of the PPO segments. From the measurements of dynamic mechanical properties and x-ray diffraction patterns of these ionenes and their 7,7,8,8-tetracyanoquinodimethane (TCNQ) salts, a microheterogeneous structure of the PPO segments and the polycation-TCNQ salts segments in the TCNQ salts was estimated. On the basis of this microstructure a change in the conductive and dielectric properties with an increase on the weight fraction of the PPO segments the TCNQ salts (Wf) were discussed. For the simple salts the values of resistivity (ρ) and activation energy of conduction (Ea) were increased with the increase in the value of Wf. The values of ρ for the complex salts also increased with the increase in the value of Wf, whereas the values of Ea were nearly constant (ca. 0.07 eV) until the value of Wf reached 0.8. Strong interaction between and TCNQ° molecules facilitated the formation of the continuous conduction columns and did not change their structure and properties. Dielectric constant (e) of the TCNQ salts attained 102−104. The dielectric behavior was consistent with the conductive behavior, and the appearance of the high e values was caused by polarization of carrier electrons of the TCNQ salts in the conductive paths isolated or interrupted by the PPO segments. As the Wf value increased, the e values of the TCNQ salts decreased. The decrease in the number of these paths accompanied by the increase in the Wf value led to reduced e values.
- Published
- 1982
19. Anisotropic electrical conductivity of drawn elastomeric ionene–TCNQ salts
- Author
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Isao Shinohara, Yoshio Takizawa, and Masayoshi Watanabe
- Subjects
Materials science ,Condensed matter physics ,Structural change ,Electrical resistivity and conductivity ,Perpendicular ,Activation energy ,Anisotropy ,Elastomer ,Microstructure ,Thermal conduction - Abstract
Elastomeric ionene–TCNQ salts with favorable electrical, mechanical, and processing characteristics were drawn mechanically. The electrical conductivity parallel and perpendicular to the drawing axis was investigated. Correlation between anisotropic conductivity and the change in microstructure was discussed. The resistivity ρ at 25°C of the simple salt (EI-TCNQ0) and the complex salt (EI-TCNQ0.5) were on the order of 105 and 102 Ω cm, respectively. In the drawn TCNQ salts, the ρ parallel to the drawing axis increased greatly; on the other hand, the ρ perpendicular to this axis increased slightly or was similar to the ρ of the undrawn TCNQ salts. The anisotropy in the ρ of EI-TCNQ0.5 between the two directions reached 40 times. The activation energy also increased in the direction parallel to the drawing axis. In the undrawn TCNQ salts, the continuous conduction paths exist isotropically. With drawing, the continuous conduction paths, particularly in the direction parallel to the drawing axis, break or make a structural change. The anisotropic conductivity disappeared with time in EI-TCNQ0; however, it was present in EI-TCNQ0.5 even after 200 days under ambient conditions.
- Published
- 1983
20. Effect of poly(propylene oxide) segment size on structure-property relationships in elastomeric ionene
- Author
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Masayoshi Watanabe, Yoshio Takizawa, and Isao Shinohara
- Subjects
Poly(propylene oxide) ,Materials science ,Polymers and Plastics ,Organic Chemistry ,Structure property ,Water sorption ,Elastomer ,chemistry.chemical_compound ,Hysteresis ,chemistry ,Chemical engineering ,Polymer chemistry ,Materials Chemistry ,Molecule ,Propylene oxide ,Thermal relaxation - Abstract
The dynamic mechanical, thermal scanning, stress-strain and water sorption behaviours of the elastomeric ionene consisting of ionene and poly(propylene oxide) (PPO) segments are studied. The effect of PPO segment size on the microphase-separated structure in this material is described by the change of dynamic mechanical and thermal relaxation temperatures. The mixing of the PPO segment into the ionene segment domain increases with decrease of PPO segment size and reduces the crosslinking effect of the ionene segment domain, which leads to an increase in hysteresis for loading in this material. The number of equilibrium sorbed water molecules per ionene segment increases with increase in the purity of the ionene segment domain.
- Published
- 1983
21. Primary Structure of a Non-Secretory Ribonuclease from Bovine Kidney1
- Author
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Yasushi Niwata, Reiko Nitta, Hideaki Watanabe, Akihiro Sanda, Masanori Iwama, Jaap J. Beintema, Masachika Irie, Yoshio Takizawa, and Kazuko Ohgi
- Subjects
Kidney ,biology ,RNase P ,Protein primary structure ,Active site ,Sequence (biology) ,General Medicine ,Tripeptide ,Biochemistry ,Bovine kidney ,medicine.anatomical_structure ,medicine ,biology.protein ,Ribonuclease ,Molecular Biology - Abstract
The primary structure of a non-secretory ribonuclease from bovine kidney (RNase K2) was determined. The sequence determined was VPKGLTKARWFEIQHIQPRLLQCNKAMSGV NNYTQHCKPENTFLHNVFQDVTAVCDMPNIICKNGRHNCHQSPKPVNLTQCNFIAGRYPDC RYHDDAQYKFFIVACDPPQKTDPPYHLVPVHLDKYF. The sequence homology with human non-secretory RNase, bovine pancreatic RNase, and human secretory RNase are 46, 34.6, and 32.3%, respectively. The bovine kidney RNase has two inserted sequences, a tripeptide at the N-terminus and a heptapeptide between the 113th and 114th position of bovine pancreatic RNase; on the other hand, it is deleted of the hexapeptide consisting of the 17th to the 22nd amino acid residue of RNase A. The amino acid residues assumed to be the constituents of the bovine pancreatic RNase active site are all conserved except F120 (L in RNase K2).
- Published
- 1988
22. Therapeutic Evaluation on Combination Therapy with IG-100, pH4-Treated Human Immunoglobulin Preparation for i.v. Administration, and Antibiotics Against Severe Infections
- Author
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Keizo MATSUMOTO, Toru MASAOKA, Toru NAKAMURA, Kaoru SHIMADA, Ichiro URUSHIZAKI, Yutaka KOGO, Akira SAITO, Masumi TOMIZAWA, Ichiro NAKAYANA, Chikara MIKUNI, Kazuo TAKEBE, Katsuhiro OKAMOTO, Shuichiro YOSHIDA, Katsutoshi KARIYA, Yoko TOYAMA, Tomio ONUMA, Teruo NAKAMURA, Takeshi OSONOI, Shigeru OCHIAI, Morio SAGARA, Shigetoshi YANAGIYA, Osamu UEHARA, Naoyoshi MASAKI, Toyokazu TAMURA, Masao TAMURA, Takashi ITO, Yoshikatsu NEMOTO, Kiyoshi KONNO, Kotaro OIZUMI, Akira WATANABE, Shigeo KARIYONE, Tatsumi UCHIKA, Shin MATSUDA, Tadashi MAEKAWA, Shogo SHINONOME, Yasusada MIURA, Shinobu SAKAMOTO, Akihiro TSUBOYAMA, Shiro MIWA, Tadashi MIYAHARA, Jingoro SHIMADA, Hiroichi TANIMOTO, Yoshitaka NAKAMORI, Naohiko CHONABAYASHI, Hideyo KATSUNUMA, Yoshinori MIYAMOTO, Junzaburo KABE, Yasufumi MIYAMOTO, Kazuko OKABE, Keimei MASHIMO, Sumio YAMAOKA, Tetsuro UKAI, Katsunori UENO, Keiichi NAKAGAWA, Kohjin KIN, Fukuo IIJIMA, Takeshi ABE, Tadatoshi KINOSHITA, Jyuzo MATSUDA, Kazuo KAWASUGI, Toshiro OYAMA, Ichita AMAKI, Toshiteru OSHIMA, Hiroshi TAKEO, Hiroyuki KOBAYASHI, Hiroaki TAKEDA, Shin KAWAI, Hideo TERADA, Shoji HAGIWARA, Haruo NIIKURA, Kazuhiko MATSUNO, Hiraku MORI, Kunikane KIN, Yoshio TAKIZAWA, Ippei FUJIMORI, Yoshio KOBAYASHI, Akio ONAKA, Hiroshi NAKAMURA, Akira SHIBATA, Yoshiaki MORIYAMA, Hajime TAKEDA, Osamu SEKINE, Kaoru OYAMA, Michiko KANAKI, Kenichi HATTORI, Takashi YOSHIDA, Toshihiko TAKEUCHI, Masahito KATO, Toshiyuki YAMAMOTO, Kanzo SUZUKI, Hidekazu HANAKI, Motoko YAMAMOTO, Jiro YURA, Nagao SHINAGAWA, Tetsuro TAKAOKA, Akishige NAKAMURA, Yutaka HIROTA, Yoshihisa FUJIWARA, Masataka SASADA, Akemi KUBO, Tsuyoshi YONEZAWA, Yoshio KANAYAMA, Hirotoshi SHIBATA, Katsuji SAKAI, Takami UEDA, Teruo KITANI, Ichiro KONISHI, Kojiro YASUNAGA, Yuruko OKAMOTO, Keigo MAEHARA, Yoshihiro UEDA, Atsushi HORIUCHI, Hirofumi HASEGAWA, Haruto UCHINO, Hiroyoshi SAWADA, Shiro NAKAYAMA, Kenichi NAGAI, Kiyoyasu NAGAI, Akihisa KANAMURA, Soichiro YOSHIYASU, Takao HATTORI, Minoru NIIMOTO, Yukihisa MIYOSHI, Sadanori HAMAMOTO, Minoru TANADA, Hideyuki NAKANE, Rinzo SOEJIMA, Yoshito NIKI, Chikara NAKAHAMA, Toshio KANEKO, Kenji SHINOHARA, Kohei KAKU, Eiro TSUBURA, Masakazu TAMURA, Tomohiro KUSABA, Yoshiyuki NIHO, Seiichi OKAMURA, Masahide TAKII, Michio ONO, Kohei HARA, Atsushi SAITO, Keizo YAMAGUCHI, Yoji SUZUYAMA, Yoshiteru SHIGENO, Hiroshi TOMITA, Masao NAGASAWA, Michito ICHIMARU, Shuichi IKEDA, Tomoyuki HARADA, Tsuyoshi NAGATAKE, Shukuro ARAKI, Masayuki Ando, Mineharu SUGIMOTO, and Moritaka SUGA
- Subjects
I v administration ,Combination therapy ,medicine.drug_class ,business.industry ,Clinical investigation ,Antibiotics ,Immunology ,medicine ,General Medicine ,Therapeutic evaluation ,business ,Human immunoglobulin - Published
- 1984
23. Long-term Follow-up of Hepatitis using Computed Tomography
- Author
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Keiichi Hirata, Yoshio Takizawa, Shigeyuki Hayashi, Sinya Nakagawa, Toshiyuki Ishikawa, Takao Obara, and Nobuyoshi Ishikawa
- Subjects
Adult ,medicine.medical_specialty ,Time Factors ,Hepatitis, Viral, Human ,Scintigraphy ,Muscle hypertrophy ,Atrophy ,Ascites ,medicine ,Humans ,Radiology, Nuclear Medicine and imaging ,Hepatitis, Chronic ,Hepatitis ,Hyperplasia ,medicine.diagnostic_test ,business.industry ,Hepatitis C ,Hepatitis B ,medicine.disease ,Liver regeneration ,Liver Regeneration ,Liver ,Female ,Radiology ,medicine.symptom ,Tomography, X-Ray Computed ,business ,Follow-Up Studies - Abstract
Computed tomography of the liver was performed on two patients with subacute hepatitis. The CT findings included the presence of multiple regenerative nodules in the atrophied liver, shown by decreased CT attenuation. Complications due to hepatitis, such as massive ascites and splenomegaly, were also observed. The CT observations during the course of the disease suggested that the hepatic necrosis had been repaired by hypertrophy of regenerating nodules, not by an increase in the number of nodules, which ultimately gave rise to postnecrotic cirrhosis. Scintigraphy confirmed atrophy and repair of the liver. Thus, CT and scintigraphy were considered to be useful for the diagnosis of extensive hepatic necrosis and for evaluating the process of liver repair.
- Published
- 1989
24. The Characteristics and Applications of Recently Improved HASTELLOY Alloys
- Author
-
Yoshio Takizawa, Yoshida Takeshi, and Ichiro Sekine
- Subjects
General Engineering ,General Materials Science - Published
- 1982
25. Modification of a Ribonuclease from Rhizopus Sp. with 1-Cyclohexyl-3-(2-Morpholinyl-(4)-Ethyl)Carbodiimide p-Toluenesulfonate
- Author
-
Yoshio Takizawa, Akihiro Sanda, Masachika Irie, and Masanori Iwama
- Subjects
musculoskeletal diseases ,Protein Conformation ,RNase P ,Stereochemistry ,Cytidine ,macromolecular substances ,Biochemistry ,chemistry.chemical_compound ,Ribonucleases ,Hydrolase ,Ribonuclease ,Molecular Biology ,Carbodiimide ,chemistry.chemical_classification ,Binding Sites ,biology ,Circular Dichroism ,technology, industry, and agriculture ,Active site ,Chemical modification ,General Medicine ,Hydrogen-Ion Concentration ,CME-Carbodiimide ,Adenosine Monophosphate ,Peptide Fragments ,Amino Acids, Dicarboxylic ,Carbodiimides ,Kinetics ,Enzyme ,chemistry ,biology.protein ,Rhizopus - Abstract
The carboxyl group in a ribonuclease from Rhizopus sp. (RNase Rh) was modified by a water-soluble carbodiimide, 1-cyclohexyl-3-(2-morpholinyl-(4)-ethyl)carbodiimide p-toluenesulfonate (CMC). From the relation between the extent of modification and the enzymatic activity, it was concluded that at least the modification of two carboxyl groups seemed to induce the loss in enzymatic activity. In the presence of 1 M cytidine, RNase Rh activity was protected from the CMC-modification. Under conditions in which the enzyme was inactivated to 20% activity, about 70% of the enzymatic activity was retained in the presence of cytidine. The inactivation of the RNase Rh pre-treated with CMC in the presence of cytidine with [14C]CMC indicated that the RNase Rh lost its enzymatic activity with the incorporation of about one [14C]CMC. Therefore, it could be concluded that one carboxyl group is involved in the active site of RNase Rh. The binding of the CMC-modified RNase Rh with 2'-AMP was studied spectrophotometrically. The affinity of the modified RNase Rh towards 2'-AMP decreased markedly upon CMC modification.
- Published
- 1985
26. [Untitled]
- Author
-
Haruo Niikura, Hiroshi Mohri, Shoji Hagiwara, Yoshio Takizawa, Hiraku Mori, Kunikane Kim, Kazuhiko Matsuno, and Hideo Terada
- Subjects
chemistry.chemical_compound ,Chromatography ,Glucoside ,Platelet aggregation ,Biochemistry ,Chemistry ,Template Bleeding Time ,Platelet ,General Medicine ,Function (biology) - Published
- 1983
27. [Untitled]
- Author
-
Hideo Terada, Yoshio Takizawa, Hiraku Mori, Masayo Furukawa, Kunikane Kin, Haruo Niikura, Shoji Hagiwara, and Chikako Iwabuchi
- Subjects
Biochemistry ,Platelet aggregation ,Chemistry ,Adenine nucleotide ,Platelet ,General Medicine ,Function (biology) - Published
- 1984
28. Isolation and characterization of protease modified ribonucleases from Rhizopus sp
- Author
-
Kazuko Ohgi, Eiji Wakabayashi, Masachika Irie, Akihiro Sanda, Sachiko Mine, and Yoshio Takizawa
- Subjects
Gel electrophoresis ,chemistry.chemical_classification ,Protease ,biology ,Chemistry ,RNase P ,medicine.medical_treatment ,Hydrolysis ,Size-exclusion chromatography ,General Chemistry ,General Medicine ,biology.organism_classification ,RNase PH ,Amino acid ,Molecular Weight ,Ribonucleases ,Rhizopus ,Biochemistry ,Drug Discovery ,biology.protein ,medicine ,Electrophoresis, Polyacrylamide Gel ,Ribonuclease ,Peptide Hydrolases - Abstract
In order to clarify the reason for the variation in specific activities of ribonuclease preparations from Rhizopus sp. ribonuclease (RNase Rh), low specific activity species (RNase Rh') were separated from native RNase Rh by DEAE Toyopearl 650 column chromatography and characterized. When RNase Rh' was subjected to gel electrophoresis in the absence of 2- mercaptoethanol, it gave a 24 kilodalton (kDa) protein band, but in the presence of the reducing agent it gave 17 and 7 kDa bands. These two peptides were separated by gel filtration and their NH2-terminal amino acid sequences were determined. The results indicated that RNase Rh' was an enzyme species cleaved at about the 50th residue of native RNase Rh by proteases during the course of purification, but the two fragments were still covalently joined by S-S bridges. RNase Rh' retained about 70% of the native activity and has a similar conformation to the native enzyme.
- Published
- 1987
29. Purification of acid ribonucleases from bovine spleen
- Author
-
Masachika Irie, Yoshio Takizawa, Kazuko Ohgi, and Akihiro Sanda
- Subjects
Poly U ,Immunodiffusion ,Glycoside Hydrolases ,RNase P ,Biochemistry ,Sepharose ,Gel permeation chromatography ,Ribonucleases ,Animals ,Ribonuclease ,Amino Acids ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,Chromatography ,biology ,Molecular mass ,Hydrolysis ,General Medicine ,Hydrogen-Ion Concentration ,Amino acid ,Molecular Weight ,Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase ,Poly C ,chemistry ,biology.protein ,Pancreatic ribonuclease ,Cattle ,Electrophoresis, Polyacrylamide Gel ,Spleen - Abstract
Two acid RNases were purified from bovine spleen by means of ammonium sulfate fractionation, chromatographies on-phospho-cellulose, heparin-Sepharose CL-6B, poly G-Sepharose, and 2', 5'-ADP-Sepharose, and gel filtration on Toyopearl HW 55F. Both purified preparations were homogeneous as judged by disc electrophoresis at pH 4.3. They were designated as RNase BSP1 and RNase BSP2 in the order of elution from a phospho-cellulose column. RNase BSP2 was immunologically indistinguishable from RNase K2 from bovine kidney. RNase BSP1 was a typical pyrimidine base-specific, uridylic acid-preferential RNase and had very sharp pH optimum at 6.5. RNase BSP1 thus obtained was a glycoprotein giving two major bands on SDS-slap electrophoresis. Although the apparent molecular weight of RNase BSP1 was distributed in the range of 27,000-20,000, it decreased to about 17,000-18,000 after endoglycosidase F digestion. The N-terminal amino acid sequence up to the 20th amino acid had no homology to those of RNase K2 and RNase A.
- Published
- 1988
30. Purification and properties of bovine kidney ribonucleases
- Author
-
Akihiro Sanda, Kazuko Ohgi, Yoshio Takizawa, Yasushi Niwata, and Masachika Irie
- Subjects
Immunodiffusion ,Chemical Phenomena ,RNase P ,Carbohydrates ,Kidney ,Biochemistry ,Substrate Specificity ,Ribonucleases ,Hydrolase ,Animals ,Ribonuclease ,Amino Acids ,Molecular Biology ,chemistry.chemical_classification ,Autoanalysis ,Edman degradation ,biology ,Molecular mass ,Tryptophan ,General Medicine ,Hydrogen-Ion Concentration ,Molecular biology ,Molecular Weight ,Chemistry ,Enzyme ,chemistry ,Solubility ,Sephadex ,biology.protein ,Chromatography, Gel ,Cattle ,Electrophoresis, Polyacrylamide Gel - Abstract
Two RNases (RNases K1 and K2) were purified from bovine kidney by means of column chromatography on phospho-cellulose, Sephadex G-50, CM-cellulose, heparin-Sepharose, nd agarose-APUP. They were named RNase K1 and RNase K2 in order of elution from the heparin-Sepharose column. The purity of RNase K1 thus obtained was about 90% by SDS-disc electrophoresis. RNase K2 was purified to homogeneity by SDS- and pH 4.3 disc electrophoresis. The yield of RNase K2 was 3.4 mg from 11 kg of kidneys. The antigenic properties of the two bovine renal RNases were studied by Ouchterlony's double diffusion analysis. RNase K1 and RNase A were serologically indistinguishable. RNase K2 did not cross-react immunologically with RNase K1 or RNase A. The molecular weights of these RNases determined by gel-filtration on Sephadex G-50 were 13,400 and 14,600 for RNase K1 and RNase K2, respectively. The pH optima for RNase K1 and RNase K2 were 8.5 and 6.5, respectively. Both RNase K1 and RNase K2 were as acid stable as RNase A. RNase K2 was less heat-stable than RNase K1 and RNase A. Although both renal RNases were pyrimidine nucleotide-specific enzymes, RNase K1 and RNase A were more preferential or cytidylic acid than RNase K2. The chemical composition of RNase K2 was determined. RNase K2, like human urinary RNase Us, contained one tryptophan residue. The N-terminal sequences of RNase K2 and RNase Us were determined by Edman degradation. Rnase K2 had a homologous sequence of about 10 amino acid residues with the sequence of RNase Us, a typical non-secretory RNase, within the N-terminal 30 residues.
- Published
- 1985
31. Corrosion of High-lebel Waste Containers
- Author
-
Yoshio Takizawa
- Subjects
Metallurgy ,General Engineering ,Environmental science ,General Materials Science ,Corrosion - Published
- 1983
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