Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Yoichi Ohba"'
Publikováno v:
Journal of Organometallic Chemistry. 687:436-443
Dinuclear palladium complexes bridged by a novel PNNP ligand, N,N ′-bis[(2-diphenylphosphino)phenylformamidinate (dpfam), were found to be very efficient and selective catalysts for the double carbonylation of iodobenzene with diethylamine using K
Autor:
Kojiro Takahashi, Masaharu Takigawa, Fujio Suzuki, Tomoyuki Hisa, Yoichi Ohba, Yuso Goto, Yusuke Kimura
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1245:1-8
We previously reported that a novel human chondrosarcoma-derived chondrocytic cell line, HCS-2/8, produced an anti-tumor angiogenesis factor and secreted it into the culture medium [Takigawa et al.: Anticancer Res., 10, 311-316, 1990]. In the present
Autor:
Hideya Hayashi, Makiko Mizunuma, Kouhei Tsumoto, Satoru Misawa, Mitsuhiro Matsumoto, Izumi Kumagai, Nobuhiro Kasai, Yoichi Ohba, Takamasa Ueno
Publikováno v:
Journal of virology. 74(14)
A series of mouse monoclonal antibodies (MAbs) to the nonstructural protein 3 (NS3) of hepatitis C virus was prepared. One of these MAbs, designated 8D4, was found to inhibit NS3 protease activity. This inhibition was competitive with respect to the
Publikováno v:
Applied Microbiology and Biotechnology. 37
Rhodococcus rhodochrous PA-34 isolated from soil as a propionitrile-utilizing microorganism, hydrolysed several α-aminonitriles to optically active amino acids. The hydrolysis of α-aminonitriles was found to be catalysed by a nitrilase. The charact
Autor:
Ryo Muramatsu, Tek Chand Bhalla, Akiko Wakamoto, Keizo Furuhashi, Yoichi Ohba, Miho Aoshima, Akira Miura
Publikováno v:
Biochemical Engineering for 2001 ISBN: 9784431681823
The α-aminonitriles are used as intermediates in the chemical synthesis of racemic amino acids and appear to be potentially attractive substrates for their hydrolysis to amino acids by microbial nitrilases. Although the production of L-alanine by Ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85c28c3194d1a4d1df6a5393294c9307
https://doi.org/10.1007/978-4-431-68180-9_61
https://doi.org/10.1007/978-4-431-68180-9_61
Autor:
Yusuke Mizuno, Hiroyuki Shiokawa, Yoshikazu Kanesaka, Takiko Tamura, Hisakazu Fujita, Yoichi Ohba
Publikováno v:
Archives of biochemistry and biophysics. 278(2)
Distributions of acylphosphatase isozymes among organs of several animal species were investigated. Organ extracts of pig and chicken were treated with isozyme-specific antibodies, subjected to electrophoresis on a polyacrylamide gel, then the gel wa
Publikováno v:
The Journal of Biochemistry. 102:1221-1229
The amino acid sequence of one, Ch2, of the two isozymes of chicken muscle acylphosphatase was determined. It consists of 98 amino acid residues with N-acetylalanine at the amino(N)-terminus and contains no cysteine: Ac-Ala-Gly-Ser-Glu- Gly-Leu-Met-S
Publikováno v:
The Journal of Biochemistry. 102:1213-1220
The amino acid sequence of chicken muscle acylphosphatase isozyme Ch1 was determined. The protein consists of 102 amino acid residues, does not contain histidine, and the NH2-terminus is acetylated: Ac-Ser-Ala-Leu-Thr-Lys-Ala-Ser-Gly-Ser- Leu-Lys-Ser
Publikováno v:
The Journal of Biochemistry. 105:173-177
Activities of the two isozymes, Ch1 and Ch2, of chicken muscle acylphosphatase were measured in breast muscles, leg muscles, and livers of developing chicks from day 11 in ovo to day 15 of free life. Measurement was performed using rabbit antibodies
Publikováno v:
The Journal of Biochemistry. 98:909-919
Two acylphosphatases, named Ch1 and Ch2, have been purified from chicken skeletal muscle. The molecular weights were determined to be 11,900 and 12,000 for Ch1 and Ch2, respectively, by sedimentation equilibrium. In the amino acid compositions of Ch1