Výsledky vyhledávání - "Tsukimi Iida"

Thermodynamic stability of human lipocalin-type prostaglandin D synthase under various pH conditions

Autor: Tsukimi Iida, Masatoshi Nakatsuji, Yoshiaki Teraoka, Yuji Goto, Takaki Yamamura, Takashi Inui

Publikováno v: The Journal of Biochemistry.

Lipocalin-type prostaglandin D synthase (L-PGDS) binds various hydrophobic small molecules. Since we aim to use human L-PGDS as a carrier in a drug delivery system (DDS) for poorly water-soluble drugs, quality control of the protein is indispensable.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::15237a701e90b4e261c6d92b42fede58
https://doi.org/10.1093/jb/mvad016

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Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase

Autor: Maki Mochizuki, Tadayasu Ohkubo, Susumu Uchiyama, Tsukimi Iida, Shigenori Nishimura, Akiyoshi Tanaka, Yoshihiro Urade, Takashi Inui

Publikováno v: FEBS Journal. 275:233-241

Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) is a dual-functioning protein in the lipocalin family, acting as a PGD(2)-synthesizing enzyme and as an extracellular transporter for small lipophilic molecules. We earlier reported that denaturan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::49ce608d3e89be2f4971904b9a1bd2f3
https://doi.org/10.1111/j.1742-4658.2007.06193.x

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NMR and CD analysis of an intermediate state in the thermal unfolding process of mouse lipocalin-type prostaglandin D synthase

Autor: Tsukimi Iida, Yasuo Noda, Shin-ichi Segawa, Yuya Miyamoto, Akiyoshi Tanaka, Keisuke Yamaguchi, Takashi Inui, Shigenori Nishimura

Publikováno v: Journal of biochemistry. 151(3)

We previously reported that the thermal unfolding of mouse lipocalin-type prostaglandin D synthase (L-PGDS) is a completely reversible process under acidic conditions and follows a three-state pathway, including an intermediate state (I) between nati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16f5209e8555c421331d3977ee83852c
https://pubmed.ncbi.nlm.nih.gov/22210903

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Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase

Autor: Tsukimi, Iida, Shigenori, Nishimura, Maki, Mochizuki, Susumu, Uchiyama, Tadayasu, Ohkubo, Yoshihiro, Urade, Akiyoshi, Tanaka, Takashi, Inui

Publikováno v: The FEBS journal. 275(2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f0257eefe45195353014b768242a27bb
https://pubmed.ncbi.nlm.nih.gov/18076651

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Further application of a two-step heparin affinity chromatography method using divalent cations as eluents: purification and identification of membrane-bound heparin binding proteins from the mitochondrial fraction of HL-60 cells

Autor: Takashi Inui, Nobuyuki Uozumi, Katsuyuki Imai, Masaharu Kamo, Tsukimi Iida

Publikováno v: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences. 823(2)

Membrane proteins were obtained from the mitochondrial fraction of HL-60 cells by solubilization with octyl glucoside and bound to heparin-gels. Bound proteins were successively eluted with solutions containing increasing concentrations of Mg(2+) in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d09513e9bc02d5e3aa71b42f7f35d174
https://pubmed.ncbi.nlm.nih.gov/16019269

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2P075 Thermal Stability and Unfolding Mechanism of Human Lipocalin-type Prostaglandin D Synthase(The 48th Annual Meeting of the Biophysical Society of Japan)

Autor: Satoshi Kume, Tsukimi Iida, Takashi Inui, Shigenori Nishimura, Kaoru Saruwatari, Harumi Fukuda

Publikováno v: Seibutsu Butsuri. 50:S95

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::002797edd9ea07c64c9ded8e1f6004b2
https://doi.org/10.2142/biophys.50.s95_2

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