Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Norio Inokuchi"'
Autor:
Keiichi Tabata, Yukinaga Kishikawa, Eiji Kose, Megumi Izumisawa, Yoshihisa Ito, Satoru Asami, Takashi Suzuki, Norio Inokuchi, Harumi Hata, Shin-ichi Ono, Hiroyuki Hayashi, Kumiko Ishige, Yasuhiro Kosuge, Hiroko Kobayashi
Publikováno v:
YAKUGAKU ZASSHI. 137:1419-1423
It has been recommended that active learning methods, such as team-based learning (TBL) and problem-based learning (PBL), be introduced into university classes by the Central Council for Education. As such, for the past 3 years, we have implemented T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1f91be28ac25abe52c69e35608158d4
https://doi.org/10.1248/yakushi.17-00094
https://doi.org/10.1248/yakushi.17-00094
Publikováno v:
Mycoscience. 56:523-529
The gene encoding the RNase T2 family enzyme, RNMel36, was cloned from Mortierella elongata (Zygomycota, Mortierellales) by polymerase chain reaction. The deduced protein sequence contains a signal sequence, catalytic domain, S/T rich domain and an e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41931ea1460d9c566e0661272e55070b
https://doi.org/10.1016/j.myc.2015.04.001
https://doi.org/10.1016/j.myc.2015.04.001
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 79:211-217
RNase He1 from Hericium erinaceus, a member of the RNase T1 family, has high identity with RNase Po1 from Pleurotus ostreatus with complete conservation of the catalytic sequence. However, the optimal pH for RNase He1 activity is lower than that of R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b56c55663ab88775af8863bf15bdcdf
https://doi.org/10.1080/09168451.2014.972327
https://doi.org/10.1080/09168451.2014.972327
Publikováno v:
Biological and Pharmaceutical Bulletin. 37:1843-1847
Here, we determined the sequence of a cDNA encoding a guanylic acid-specific ribonuclease (RNase He1) from Hericium erinaceus that exhibits high sequence identity (59%) with RNase Po1, an enzyme with anti-cancer activity and which is found in Pleurot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c4bb2f17081582576cef8b77d9b3604
https://doi.org/10.1248/bpb.b14-00553
https://doi.org/10.1248/bpb.b14-00553
Autor:
Keiichi Tabata, Naomi Motoyoshi, Hiroko Kobayashi, Takashi Suzuki, Tadashi Itagaki, Norio Inokuchi
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 77:1486-1491
RNase Po1 is a guanylic acid-specific ribonuclease (a RNase T1 family RNase) from Pleurotus ostreatus. We determined the cDNA sequence encoding RNase Po1 and expressed RNase Po1 in Escherichia coli. A comparison of the enzymatic properties of RNase P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13d7c17c6f172651e68017a6c6e867a3
https://doi.org/10.1271/bbb.130133
https://doi.org/10.1271/bbb.130133
Publikováno v:
Mycoscience. 54:188-197
A gene encoding a ribonuclease T2 (RNase T2) family enzyme, RNHe30, was cloned from Hericium erinaceum by PCR. The deduced amino acid sequence from the complimentary DNA (cDNA) (1074 bp) encodes a 302-aa protein (RNase He30) that has the consensus am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f027bb53541eaf1b1d44046ac2ae8239
https://doi.org/10.1016/j.myc.2012.09.011
https://doi.org/10.1016/j.myc.2012.09.011
Amino acid sequence analysis and characterization of a ribonuclease from starfish Asterias amurensis
Publikováno v:
Journal of biochemistry. 160(3)
The aim of this study was to phylogenetically characterize the location of the RNase T2 enzyme in the starfish (Asterias amurensis). We isolated an RNase T2 ribonuclease (RNase Aa) from the ovaries of starfish and determined its amino acid sequence b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f5fd8d36ae971e0b50bf43311a748f9
https://pubmed.ncbi.nlm.nih.gov/26920046
https://pubmed.ncbi.nlm.nih.gov/26920046
Publikováno v:
Journal of Liquid Chromatography & Related Technologies. 34:182-194
Partition efficiency of the high-pitch locular multilayer coil was evaluated in countercurrent chromatographic (CCC) separation of proteins with an aqueous-aqueous polymer phase system using the small-scale cross-axis coil planet centrifuge (X-axis C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::225040a2e5f88f1772a72deb627031c4
https://doi.org/10.1080/10826076.2011.546151
https://doi.org/10.1080/10826076.2011.546151
Publikováno v:
Iryo Yakugaku (Japanese Journal of Pharmaceutical Health Care and Sciences). 29:732-739
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e6c8e4a1b0cd8de4dccb121f470f080
https://doi.org/10.5649/jjphcs.29.732
https://doi.org/10.5649/jjphcs.29.732
Autor:
Norio Inokuchi, Hiroko Kobayashi, Kazuko Ohgi, Tadashi Itagaki, Masachika Irie, Masanori Iwama, Tatsuya Wada
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 67:2307-2310
Two new RNase T2 Ribonucleases, RNase Le37 and Irp3, with a molecular mass of 45 kDa, have been isolated from Basidiomycetes fungi, Lentinus edodes and Irpex lacteus, respectively. The ribonucleases consisted of three domains: an RNase active domain,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b82822dd4ed6dbeeb8877f9e733ae416
https://doi.org/10.1271/bbb.67.2307
https://doi.org/10.1271/bbb.67.2307