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Author Kondo, Yuki| Rikiishi, Kazuhide| Sugimoto, Manabu|
Keywords 8-oxo-dGTP nudix hydrolase Oryza sativa transcriptional error UV-C
Published Date 2022-09
Publication Title Antioxidants
Volume volume11
Issue issue9
Publisher MDPI
Start Page 1805
ISSN 2076-3921
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
Copyright Holders © 2022 by the authors.
File Version publisher
PubMed ID 36139879
DOI 10.3390/antiox11091805
Web of Science KeyUT 000858199700001
Related Url isVersionOf https://doi.org/10.3390/antiox11091805
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Author Sugimoto, Manabu| Watanabe, Toshiro| Takaoka, Motoko| Suzuki, Kyoko| Murakami, Tadatoshi| Murakami, Nobutada| Sumikawa, Shoichi|
Keywords fermented plant extract microbiota dextran sulfate sodium inflammatory Clostridiales
Published Date 2021-04-06
Publication Title Fermentation-Basel
Volume volume7
Issue issue2
Publisher MDPI
Start Page 55
ISSN 2311-5637
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
Copyright Holders © 2021 by the authors.
File Version publisher
DOI 10.3390/fermentation7020055
Web of Science KeyUT 000665199500001
Related Url isVersionOf https://doi.org/10.3390/fermentation7020055
FullText URL fulltext20210616-1.pdf
Author Rikiishi, Kazuhide| Sugimoto, Manabu| Maekawa, Masahiko|
Keywords mutant seed development seed dormancy transcriptome wheat
Published Date 2021-02-17
Publication Title Breeding Science
Volume volume71
Issue issue2
Publisher Japanese Society of Breeding
Start Page 155
End Page 166
ISSN 1344-7610
NCID AA11353132
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
File Version publisher
NAID 130008040484
DOI 10.1270/jsbbs.20016
Web of Science KeyUT 000654086400005
Related Url isVersionOf https://doi.org/10.1270/jsbbs.20016
Author Fujitani, Yoshiyuki| Horiuchi, Terumi| Ito, Kazutoshi| Sugimoto, Manabu|
Published Date 2007-6
Publication Title PHYTOCHEMISTRY
Volume volume68
Issue issue11
Content Type Journal Article
Title Alternative ホウレンソウ種子に存在するα-グルコシダーゼの分子多型変化
FullText URL 005_001_001_009.pdf
Author Furui, Satoshi| Sugimoto, Manabu| Suzuki, Yukio|
Abstract Two molecular forms of α-glucosidase were isolated from spinach seeds after storage at 4℃ by CM-cellulose column chromatography and gel filtration. The molecular masses of α-glucosidase A and B were 78 kDa and 82 kDa by SDS-PAGE, and 62 kDa and 70 kDa by gel filtration, respectively. α-Glucosidase A had high activity not only toward maltooligosaccharides but also toward α-glucans. The optimum pH was 4.5-5.5 and about 50% of the activity remained after incubation at 65℃ for 20 min. On the other hand, α-glucosidase B had high activity toward maltooligosaccharides but faint activity toward α-glucans. The optimum pH was 5.0 and no activity was found after incubation at 65℃ for 20 min. The enzymatic and immunological properties of α-glucosidase A and B were similar to those of α-glucosidase. Ⅰor Ⅱ, and α-glucosidase Ⅲ or Ⅳ, isolated from spinach seeds without 4℃ storage, respectively. These findings suggest that the α-glucosidase in spinach seeds is modified to be two molecular forms.
Keywords Spinach α-Glucosidase Multiple molecular forms
Publication Title 岡山大学資源生物科学研究所報告
Published Date 1997
Volume volume5
Issue issue1
Start Page 1
End Page 9
ISSN 0916-930X
language English
File Version publisher
Title Alternative シロイヌナズナ由来過酸化リン脂質グルタチオンペルオキシダーゼ様遺伝子のクローニングと発現
FullText URL 005_002_145_153.pdf
Author Sugimoto, Manabu| Kawai, Fusako|
Abstract A cDNA encoding Arabidopsis purative phosphplipid hydroperoxide gultathione peroxidase (PHGPX) was cloned and sequenced by the reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends methods. The cDNA comprised 803 bp, and included an open reading frame which encodes a polypeptide of 169 amino acid residues with a molecular mass of 18,600 Da. The deduced amino acid sequence showed homology to plant putative PHGPXs and mammalian PHGPXs. The cloned gene was expressed in Escherichia coli cells to prouce an extra protein, which showed a molecular mass similar to the deduced one.
Keywords Arabidopsis Phospholipid hydroperoxide glutathione peroxidase Nucleotide sequence Gene expression
Publication Title 岡山大学資源生物科学研究所報告
Published Date 1998
Volume volume5
Issue issue2
Start Page 145
End Page 153
ISSN 0916-930X
language English
File Version publisher
Title Alternative Purification and Characterization of α-Glucosidases from Spinach Seeds
FullText URL 004_002_239_252.pdf
Author Sugimoto, Manabu| Furui, Satoshi| Suzuki, Yukio|
Abstract Four molecular forms of α-glucosidase were isolated from spinach seeds by several kinds of chromatography. The molecular masses of α-glucosidases Ⅰ,Ⅱ,Ⅲ,and Ⅳ were 78,78,82 and 82kDa by SDS-PAGE, and 62,62,190,and 70kDa by gel filtration, respectively. α-Glucosidases Ⅰand Ⅱ showed similar enzymatic properties. The Km for soluble starch was about 10 times lower than that for maltose, and they had higher activity not only towards malto-oligosaccharides but also towards α-glucans. The optimum pH was 4.5-5.5 and about 50% of the activity remained after incubation at 71℃ for 20 min. On the other hand, α-glucosidases Ⅲ and Ⅳ showed similar enzymatic propreties. The Km for maltose was 3-4 times lower than for solble starch, and they had high activity toward malto-oligosaccharides but faint activity towards α-glucnas. The optimum pH was 4.5-5.0 and no activity was found after incubation at 70℃ for 20 min. However, anti-α-glucosidase Ⅲ serum precipitated specifically with α-glucosidase Ⅲ.
Keywords α-Glucosidase Spinach Seed Spinacia oleracea L. Molecular form
Publication Title 岡山大学資源生物科学研究所報告
Published Date 1996
Volume volume4
Issue issue2
Start Page 239
End Page 252
ISSN 0916-930X
language Japanese
File Version publisher
Author 杉本 学|
Published Date 1994-03-25
Publication Title
Content Type Thesis or Dissertation