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- 저자 : So Kimura (검색결과 3 건)
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Yuhei Mori,Itaru Miura,Michinari Nozaki,Yusuke Osakabe,Ryuta Izumi,Takahiro Akama,So Kimura,Hirooki Yabe 대한정신약물학회 2021 CLINICAL PSYCHOPHARMACOLOGY AND NEUROSCIENCE Vol.19 No.3
Parkinson’s disease is often complicated by psychiatric symptoms. Psychiatrists are caught in a dilemma between such symptoms and physical treatment since Parkinson’s disease sometimes shows treatment resistance based on pharmacological treatment-induced dopamine dysfunction. Here, we report on a 64-year-old woman with a 15-year history of Parkinson’s disease with stage IV severity based on the Hoehn and Yahr scale. She was admitted to our hospital with a diagnosis of major depressive disorder with psychotic features. Unfortunately, her treatment course for depression was complicated by neuroleptic malignant syndrome. Because we were concerned about the persistence of her depressive symptoms, the risk of psychotropic drugs causing adverse effects, and progressive disuse syndrome, we administered modified electroconvulsive therapy. Her symptoms of neuroleptic malignant syndrome and depression sufficiently improved after five sessions of modified electroconvulsive therapy. Additionally, the primary motor symptoms of her Parkinson’s disease also markedly improved. The improvement of neuroleptic malignant syndrome and her motor symptoms based on dopamine dysfunction can be explained by electroconvulsive therapy’s effectiveness in activating dopamine neurotransmission. Besides, the marked improvement of her depressive episode with psychotic features was presumed to involve dopamine receptor activation and regulation. Because advanced Parkinson’s disease can sometimes be refractory to treatment based on pharmacological treatment-induced dopamine dysfunction, psychiatrists often have difficulty treating psychiatric symptoms; electroconvulsive therapy may stabilize the dopaminergic system in such cases, presenting a possible non-pharmacologic treatment option for Parkinson’s disease.
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Kikukawa, Takashi,Shimono, Kazumi,Tamogami, Jun,Miyauchi, Seiji,Kim, So Young,Kimura-Someya, Tomomi,Shirouzu, Mikako,Jung, Kwang-Hwan,Yokoyama, Shigeyuki,Kamo, Naoki American ChemicalSociety 2011 Biochemistry Vol.50 No.41
<P><I>Acetabularia</I> rhodopsins are the firstmicrobialrhodopsins discovered in a marine plant organism, <I>Acetabulariaacetabulum</I>. Previously, we expressed <I>Acetabularia</I> rhodopsin II (ARII) by a cell-free system from one of two opsingenes in <I>A. acetabulum</I> cDNA and showed that ARIIis a light-driven proton pump [Wada, T., et al. (2011) <I>J.Mol. Biol.</I><I>411</I>, 986–998]. In thisstudy, the photochemistry of ARII was examined using the flash-photolysistechnique, and data were analyzed using a sequential irreversiblemodel. Five photochemically defined intermediates (P<SUB><I>i</I></SUB>) were sufficient to simulate the data. Noticeably, both P<SUB>3</SUB> and P<SUB>4</SUB> contain an equilibrium mixture of M, N,and O. Using a transparent indium tin oxide electrode, the photoinducedproton transfer was measured over a wide pH range. Analysis of thepH-dependent proton transfer allowed estimation of the p<I>K</I><SUB>a</SUB> values of some amino acid residues. The estimated valueswere 2.6, 5.9 (or 6.3), 8.4, 9.3, 10.5, and 11.3. These values wereassigned as the p<I>K</I><SUB>a</SUB> of Asp81 (Asp85<SUP>BR</SUP>) in the dark, Asp92 (Asp96<SUP>BR</SUP>) at N, Glu199 (Glu204<SUP>BR</SUP>) at M, Glu199 in the dark, an undetermined proton-releasingresidue at the release, and the pH to start denaturation, respectively.Following this analysis, the proton transfer of ARII is discussed.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/2011/bichaw.2011.50.issue-41/bi2009932/production/images/medium/bi-2011-009932_0006.gif'></P>
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Production of Maltopentaose and Biochemical Characterization of Maltopentaose-Forming Amylase
KIM, YOUNG-MIN,RUY, HWA-JA,LEE, SUN-OK,SEO, EUN-SEONG,LEE, SO-YOUNG,YOO, SUM-KYUN,CHO, DONG-LYUN,KIM, DOMAN,ATSUO KIMURA,SEIYA CHIBA,LEE, JIN-HA 한국미생물 · 생명공학회 2001 Journal of microbiology and biotechnology Vol.11 No.4
Bacillus sp. AIR-5, a strain from soil, produced an extracellular maltohentaose-forming amylase from amylose and soluble starch. This bacterium produced 8.9g/l of maltopentaose from 40g/l of soluble starch in a batch fermentation and the maltopentaose made up 90% of the maltooligosaccharides produced (from maltose to maltoheptaose). The culture supernatant was concentrated using a 30K molecular weight cut-off membrane and purified by DEAE-Cellulose and Sephadex G-150 column chromatographies. The purified protein showed one band on a native-PAGE and its molecular mass was estimated as 250kDa. The 250-kDa protein was composed of tetramers of a 63-kDa protein. The isoelectric point of the purified protein was pH 6.9, and the optimum temperature for the enzyme activity was 45℃. The enzyme was quickly inactivated above 55℃, and showed a maximum activity at pH 8.5 and over 90% stability between a pH of 6 to 10. The putative N-terminal amino acid sequence of AIR-5 amylase, ATINNGTLMQYFEWYVPNDG, showed a 96% sequence similarity with that of BLA, a general liquefying amylase.
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