Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Megumi Akiyoshi-Shibata"'
Autor:
Megumi Akiyoshi-Shibata, Toshiyuki Sakaki, Shiro Kominami, Takeshi Yamazaki, Tadashi Imai, Yoshiyasu Yabusaki, Takashi Ohno
Publikováno v:
Biochemistry. 37:2800-2806
Bovine P450(17alpha,lyase) containing an additional four histidine residues at the COOH terminus was expressed in Escherichia coli and purified by one-step column chromatography using Ni-chelate resin. The membrane enzyme was incorporated into liposo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cdbd8ad3352c22719365a6d3d08089b
https://doi.org/10.1021/bi9715066
https://doi.org/10.1021/bi9715066
Publikováno v:
Journal of Biological Chemistry. 271:26209-26213
We have reported the localization on yeast microsomes for a modified P450c27 (mic-P450c27) that contains the microsomal targeting signal of bovine P450c17 in front of the mature form of rat mitochondrial P450c27 (Sakaki, T., Akiyoshi-Shibata, M., Yab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6d8f2de903e86ebd6b0ee2598c1ed4d
https://doi.org/10.1074/jbc.271.42.26209
https://doi.org/10.1074/jbc.271.42.26209
Autor:
Shigeki Takemori, Toshiyuki Sakaki, Hideo Ohkawa, Shiro Kominami, Megumi Akiyoshi-Shibata, Yoshiyasu Yabusaki
Publikováno v:
Biochemistry. 33:4933-4939
Three expression plasmids, pAMC1 for rat P4501A1, pAMR2 for P4501A1 and yeast NADPH-P450 reductase, and pAFCR1 for a fused enzyme between P4501A1 and the reductase, were constructed, and each was introduced into Saccharomyces cerevisiae AH22 cells. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea155c1fbb74641722de2df73a640d95
https://doi.org/10.1021/bi00182a023
https://doi.org/10.1021/bi00182a023
Autor:
Toshiyuki Sakaki, Hiroko Murakami, Kayo Manabe, Megumi Akiyoshi-Shibata, Hideo Ohkawa, Yoshiyasu Yabusaki
Publikováno v:
Pharmacogenetics. 1:86-93
Simultaneous expression plasmids were constructed for bovine adrenal cytochromes P450c17 and P450c21 (pA gamma alpha) and for both P450s together with NADPH-cytochrome P450 reductase (pAR gamma alpha). On introduction of each of the plasmids into Sac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0716e7ceb8e8d6a05f4f890ada819e7c
https://doi.org/10.1097/00008571-199111000-00005
https://doi.org/10.1097/00008571-199111000-00005
Publikováno v:
DNA and Cell Biology. 10:613-621
Expression of both bovine adrenodoxin (ADX) and NADPH-adrenodoxin reductase (ADR) were examined in Saccharomyces cerevisiae. Three ADX and two ADR expression plasmids were constructed by inserting each of the corresponding cDNA fragments between the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f448e6ccf2b60144db7d898c66faf41
https://doi.org/10.1089/dna.1991.10.613
https://doi.org/10.1089/dna.1991.10.613
Publikováno v:
Xenobiotica; the fate of foreign compounds in biological systems. 28(5)
1. Kidney mitochondrial 24-hydroxylase cytochrome P450 (CYP24) catalyses sequential hydroxylation at both C-24 and C-23 positions of calcidiol and calcitriol. Here, we have investigated the in vitro metabolism of a hexafluorinated derivative of calci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37dbf9fe7c31131dd1f9b821d8603b6e
https://pubmed.ncbi.nlm.nih.gov/9622848
https://pubmed.ncbi.nlm.nih.gov/9622848
Autor:
Mitsuhide Noshiro, Megumi Akiyoshi-Shibata, Kyuichiro Okuda, Yoshihiko Ohyama, Yoshiyasu Yabusaki, Emiko Usui
Publisher Summary Vitamin D 3 is hydroxylated to 25-hydroxyvitamin D 3 by a vitamin D 3 25-hydroxylase (25-hydroxylase) located in liver mitochondria or endoplasmic reticulum. 25-hydroxyvitamin D 3 is then transported to the kidney through the bloods
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52c893249c16d25e0c7486da23b74194
https://doi.org/10.1016/s0076-6879(97)82109-x
https://doi.org/10.1016/s0076-6879(97)82109-x
Publikováno v:
The Journal of biological chemistry. 267(23)
A modified rat cytochrome P450c27, whose mitochondrial targeting signal had been replaced by a possible microsomal targeting signal of bovine cytochrome P450c17, was expressed in yeast. The modified P450c27 hemoprotein was correctly localized on yeas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ee5af78e9d890f963ff4e1ea4220535
https://pubmed.ncbi.nlm.nih.gov/1322905
https://pubmed.ncbi.nlm.nih.gov/1322905
Autor:
Emiko Usui, Megumi Akiyoshi-Shibata, Hideo Ohkawa, Toshiyuki Sakaki, Kyuichiro Okuda, Mitsuhidel Noshiro, Yoshiyasu Yabusaki
Publikováno v:
FEBS letters. 280(2)
The cDNA coding for the precursor protein of rat liver mitochondrial vitamin D3 25-hydroxylase, cytochrome P450LMT25, was expressed under the control of the yeast alcohol dehydrogenase I promoter and terminator in Saccharomyces cerevisiae AH22 cells.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b6ecd958e9c4dc8b989546089e89c49
https://pubmed.ncbi.nlm.nih.gov/2013339
https://pubmed.ncbi.nlm.nih.gov/2013339