start-ver=1.4
cd-journal=joma
no-vol=11
cd-vols=
no-issue=9
article-no=
start-page=1805
end-page=
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2022
dt-pub=202209
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Rice Nudix Hydrolase OsNUDX2 Sanitizes Oxidized Nucleotides
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Nudix hydrolase (NUDX) hydrolyzes 8-oxo-(d)GTP to reduce the levels of oxidized nucleotides in the cells. 8-oxo-(d)GTP produced by reactive oxygen species (ROS) is incorporated into DNA/RNA and mispaired with adenine, causing replicational and transcriptional errors. Here, we identified a rice OsNUDX2 gene, whose expression level was increased 15-fold under UV-C irradiation. The open reading frame of the OsNUDX2 gene, which encodes 776 amino acid residues, was cloned into Escherichia coli cells to produce the protein of 100 kDa. The recombinant protein hydrolyzed 8-oxo-dGTP, in addition to dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP), as did Arabidopsis AtNUDX1; whereas the amino acid sequence of OsNUDX2 had 18% identity with AtNUDX1. OsNUDX2 had 14% identity with barley HvNUDX12, which hydrolyzes 8-oxo-dGTP and diadenosine tetraphosphates. Suppression of the lacZ amber mutation caused by the incorporation of 8-oxo-GTP into mRNA was prevented to a significant degree when the OsNUDX2 gene was expressed in mutT-deficient E. coli cells. These results suggest that the different substrate specificity and identity among plant 8-oxo-dGTP-hydrolyzing NUDXs and OsNUDX2 reduces UV stress by sanitizing the oxidized nucleotides.
en-copyright=
kn-copyright=

en-aut-name=KondoYuki
en-aut-sei=Kondo
en-aut-mei=Yuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=RikiishiKazuhide
en-aut-sei=Rikiishi
en-aut-mei=Kazuhide
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

affil-num=1
en-affil=Institute of Plant Science and Resources, Okayama University
kn-affil=

affil-num=2
en-affil=Institute of Plant Science and Resources, Okayama University
kn-affil=

affil-num=3
en-affil=Institute of Plant Science and Resources, Okayama University
kn-affil=
en-keyword=8-oxo-dGTP
kn-keyword=8-oxo-dGTP
en-keyword=nudix hydrolase
kn-keyword=nudix hydrolase
en-keyword=Oryza sativa
kn-keyword=Oryza sativa
en-keyword=transcriptional error
kn-keyword=transcriptional error
en-keyword=UV-C
kn-keyword=UV-C
END

start-ver=1.4
cd-journal=joma
no-vol=7
cd-vols=
no-issue=2
article-no=
start-page=55
end-page=
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2021
dt-pub=20210406
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Anti-Inflammatory Effect on Colitis and Modulation of Microbiota by Fermented Plant Extract Supplementation
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Although results of recent studies suggest that fermented foods strongly affect the gut microbiota composition and that they relieve inflammatory bowel disease symptoms, some reports have described that fermented foods increase some inflammation markers based on differences in fermented food materials. This study evaluated the effects of fermented plant extract (FPE) on dextran sulfate sodium (DSS)-induced colitis in mice and the effects on fecal microbiota composition in humans. Mice fed 5% FPE with 3% DSS (FPE group) showed no body weight loss, atrophy of colonic length, or bloody stool, similar to mice fed a basal diet (negative group), whereas mice fed 3% DSS (positive group) exhibited those effects. Concentrations of inflammation markers IL-6 and TNF-alpha were not significantly different between FPE and negative groups; however, those concentrations became higher in the positive group. 16S ribosomal RNA gene sequencing was used to characterize fecal microbiota in healthy women before and after 3-month FPE supplementation. The FPE supplementation induced increases in Firmicutes phyla and in Clostridiales order, which play a central role in inflammation suppression. These results suggest that FPE enhances Clostridiales growth in the gut and that it has an anti-inflammatory effect.
en-copyright=
kn-copyright=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=WatanabeToshiro
en-aut-sei=Watanabe
en-aut-mei=Toshiro
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=TakaokaMotoko
en-aut-sei=Takaoka
en-aut-mei=Motoko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=SuzukiKyoko
en-aut-sei=Suzuki
en-aut-mei=Kyoko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=MurakamiTadatoshi
en-aut-sei=Murakami
en-aut-mei=Tadatoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

en-aut-name=MurakamiNobutada
en-aut-sei=Murakami
en-aut-mei=Nobutada
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=6
ORCID=

en-aut-name=SumikawaShoichi
en-aut-sei=Sumikawa
en-aut-mei=Shoichi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=7
ORCID=

affil-num=1
en-affil=Institute of Plant Science and Resources, Okayama University
kn-affil=

affil-num=2
en-affil=Department of Food and Nutrition, Sonoda Women’s University
kn-affil=

affil-num=3
en-affil=Department of Biosphere Sciences, Kobe College
kn-affil=

affil-num=4
en-affil=Department of Biosphere Sciences, Kobe College
kn-affil=

affil-num=5
en-affil=Functional Food Creation Research Institute Co., Ltd.
kn-affil=

affil-num=6
en-affil=Functional Food Creation Research Institute Co., Ltd.
kn-affil=

affil-num=7
en-affil=Functional Food Creation Research Institute Co., Ltd.
kn-affil=
en-keyword=fermented plant extract
kn-keyword=fermented plant extract
en-keyword=microbiota
kn-keyword=microbiota
en-keyword=dextran sulfate sodium
kn-keyword=dextran sulfate sodium
en-keyword=inflammatory
kn-keyword=inflammatory
en-keyword=Clostridiales
kn-keyword=Clostridiales
END

start-ver=1.4
cd-journal=joma
no-vol=71
cd-vols=
no-issue=2
article-no=
start-page=155
end-page=166
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2021
dt-pub=20210217
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Transcriptomic analysis of developing seeds in a wheat (Triticum aestivum L.) mutant RSD32 with reduced seed dormancy
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Seed dormancy, a major factor regulating pre-harvest sprouting, can severely hinder wheat cultivation. Reduced Seed Dormancy 32 (RSD32), a wheat (Triticum aestivum L.) mutant with reduced seed dormancy, is derived from the pre-harvest sprouting tolerant cultivar, 'Norin61'. RSD32 is regulated by a single recessive gene and mutant phenotype expressed in a seed-specific manner. Gene expressions in embryos of 'Norin61' and RSD32 were compared using RNA sequencing (RNA-seq) analysis at different developmental stages of 20, 30, and 40 days after pollination (DAP). Numbers of up-regulated genes in RSD32 are equivalent in all developmental stages. However, down-regulated genes in RSD32 are more numerous on DAP20 and DAP30 than on DAP40. In central components affecting the circadian clock, homologues to the morning-expressed genes are expressed at lower levels in RSD32. However, higher expressions of homologues acting as evening-expressed genes are observed in RSD32. Homologues of Ca2+ signaling pathway related genes are specifically expressed on DAP20 in 'Norin61'. Lower expression is shown in RSD32. These results suggest that RSD32 mutation expresses on DAP20 and earlier seed developmental stages and suggest that circadian clock regulation and Ca2+ signaling pathway are involved in the regulation of wheat seed dormancy.
en-copyright=
kn-copyright=

en-aut-name=RikiishiKazuhide
en-aut-sei=Rikiishi
en-aut-mei=Kazuhide
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=MaekawaMasahiko
en-aut-sei=Maekawa
en-aut-mei=Masahiko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

affil-num=1
en-affil=
kn-affil=

affil-num=2
en-affil=Institute of Plant Science and Resources, Okayama University
kn-affil=

affil-num=3
en-affil=Institute of Plant Science and Resources, Okayama University
kn-affil=
en-keyword=mutant
kn-keyword=mutant
en-keyword=seed development
kn-keyword=seed development
en-keyword=seed dormancy
kn-keyword=seed dormancy
en-keyword=transcriptome
kn-keyword=transcriptome
en-keyword=wheat
kn-keyword=wheat
END

start-ver=1.4
cd-journal=joma
no-vol=68
cd-vols=
no-issue=11
article-no=
start-page=1530
end-page=1536
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2007
dt-pub=20076
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: gene cloning and recombinant protein characterization
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=<p>Several D-amino acids have been identified in plants.  However, the biosynthetic pathway to them is unclear.  In this study, we cloned and sequenced a cDNA encoding a serine racemase from barley which contained an open reading frame encoding 337 amino acid residues.  The deduced amino acid sequence showed significant identity to plant and mammalian serine racemases and contained conserved pyridoxal 5-phosphate (PLP)-binding lysine and PLP?interacting amino acid residues.  The purified gene product catalyzed not only racemization of serine but also dehydration of serine to pyruvate.  The enzyme requires PLP and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP, whereas mammalian serine racemase activity is increased by ATP.  In addition to the results regarding the effect of ATP on enzyme activity and the phylogenetic analysis of eukaryotic serine racemases, the antiserum against Arabidopsis serine racemase did not form a precipitate with barley and rice serine racemases.  This suggests that plant serine racemases represent a distinct group in the eukaryotic serine racemase family and can be clustered into monocot and dicot types.</p>
en-copyright=
kn-copyright=

en-aut-name=FujitaniYoshiyuki
en-aut-sei=Fujitani
en-aut-mei=Yoshiyuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=HoriuchiTerumi
en-aut-sei=Horiuchi
en-aut-mei=Terumi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=ItoKazutoshi
en-aut-sei=Ito
en-aut-mei=Kazutoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

affil-num=1
en-affil=
kn-affil=Okayama University

affil-num=2
en-affil=
kn-affil=Okayama University

affil-num=3
en-affil=
kn-affil=Plant Bioengineering Research Laboratories, Sapporo Breweries Ltd.

affil-num=4
en-affil=
kn-affil=Okayama University
en-keyword=Hordeum vulgare L.
kn-keyword=Hordeum vulgare L.
en-keyword=Oryza sativa
kn-keyword=Oryza sativa
en-keyword=Gramineae
kn-keyword=Gramineae
en-keyword=Pyridoxal 5-phosphate
kn-keyword=Pyridoxal 5-phosphate
en-keyword=Serine racemase
kn-keyword=Serine racemase
en-keyword=Serine dehydratase
kn-keyword=Serine dehydratase
en-keyword=d-Amino acid
kn-keyword=d-Amino acid
END

start-ver=1.4
cd-journal=joma
no-vol=5
cd-vols=
no-issue=1
article-no=
start-page=1
end-page=9
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=1997
dt-pub=1997
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=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
kn-title=Change in the Multiple Forms of α-Glucosidase from Spinach Seeds
en-subtitle=
kn-subtitle=
en-abstract=4℃保存したホウレンソウ種子から2種のα-グリコシダーゼをCM-セルロースカラムクロマトグラフィーとゲル濾過により精製した。α-グルコシダーゼAとBの分子量はそれぞれSDS-PAGEで78kDA、82kDa、ゲル濾過で62kDa、70kDaであった。α-グルコシダーゼAはマルトオリゴ糖だけではなく可溶性デンプンに対して強い加水分解活性を示した。至適pHは4.5-5.5であり、65℃、20分処理後に約50％の残存活性を示した。一方、α-グルコシダーゼBはマルトオリゴ等に対して強い加水分解活性を示したが、可溶性デンプンに対してほとんど活性を示さなかった。至適pHは5.0であり、65℃、20分処理後に活性を消失した。α-グルコシダーゼAとα-グルコシダーゼBは、4℃保存を行わない種子に見出されたα-グルコシダーゼ�T、�Uとα-グルコシダーゼ�V、�Wにそれぞれ酵素化学的性質、免疫化学的性質が類似していた。これらの結果、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は2種類に収束されることが示唆された。
kn-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. �Tor �U, and α-glucosidase �V or �W, 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.
en-copyright=
kn-copyright=

en-aut-name=FuruiSatoshi
en-aut-sei=Furui
en-aut-mei=Satoshi
kn-aut-name=古井聡
kn-aut-sei=古井
kn-aut-mei=聡
aut-affil-num=1
ORCID=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=杉本学
kn-aut-sei=杉本
kn-aut-mei=学
aut-affil-num=2
ORCID=

en-aut-name=SuzukiYukio
en-aut-sei=Suzuki
en-aut-mei=Yukio
kn-aut-name=鈴木幸雄
kn-aut-sei=鈴木
kn-aut-mei=幸雄
aut-affil-num=3
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学

affil-num=2
en-affil=
kn-affil=岡山大学

affil-num=3
en-affil=
kn-affil=岡山大学
en-keyword=Spinach
kn-keyword=Spinach
en-keyword=α-Glucosidase
kn-keyword=α-Glucosidase
en-keyword=Multiple molecular forms
kn-keyword=Multiple molecular forms
END

start-ver=1.4
cd-journal=joma
no-vol=5
cd-vols=
no-issue=2
article-no=
start-page=145
end-page=153
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=1998
dt-pub=1998
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=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
kn-title=Molecular Cloning,Sequencing and Expression of a cDNA Encoding Putative Phospholipid Hydroperoxide Glutathione Peroxidase from Arabidopsis thaliana
en-subtitle=
kn-subtitle=
en-abstract=シロイヌナズナから過酸化リン脂質グルタチオンペルオキシダーゼと高い相同性を持つタンパク質をコードするcDNAを単離し、その塩基配列を決定した。本遺伝子は、全長803bpからなり、169アミノ酸残基のタンパク質をコードしていた。アミノ酸配列は植物由来過酸化リン脂質グルタチオンペルオキシダーゼ様タンパク質と約80％の相同性を、哺乳類由来過酸化リン脂質グルタチオンペルオキシダーゼと約50％の相同性を示した。本遺伝子を大腸菌中で発現させた結果、遺伝子から予測される分子量をもつタンパク質が新たに生産された。
kn-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.
en-copyright=
kn-copyright=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=杉本学
kn-aut-sei=杉本
kn-aut-mei=学
aut-affil-num=1
ORCID=

en-aut-name=KawaiFusako
en-aut-sei=Kawai
en-aut-mei=Fusako
kn-aut-name=河合富佐子
kn-aut-sei=河合
kn-aut-mei=富佐子
aut-affil-num=2
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学

affil-num=2
en-affil=
kn-affil=岡山大学
en-keyword=Arabidopsis
kn-keyword=Arabidopsis
en-keyword=Phospholipid hydroperoxide glutathione peroxidase
kn-keyword=Phospholipid hydroperoxide glutathione peroxidase
en-keyword=Nucleotide sequence
kn-keyword=Nucleotide sequence
en-keyword=Gene expression
kn-keyword=Gene expression
END

start-ver=1.4
cd-journal=joma
no-vol=4
cd-vols=
no-issue=2
article-no=
start-page=239
end-page=252
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=1996
dt-pub=1996
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=Purification and Characterization of α-Glucosidases from Spinach Seeds
kn-title=ホウレンソウ（Spinacia oleracea L.）種子のαグルコシダーゼの精製とその性質
en-subtitle=
kn-subtitle=
en-abstract=α−グルコシダーゼの分子多型が各種クロマトグラフィーによりホウレンソウ種子から単離された。α−グルコシダーゼ�T、�U、�V、�Wの分子量は、それぞれSDS−PAGEにより78、78、82、82kDA、ゲル濾過のより62,62,190、70kDであった。α-グルコシダーゼ�Tと�Uは、可溶性デンプンを基質とした際のKm値がマルトースよりも約10倍低く、さらに、α−グルカンだけでなくマルトオリゴ糖に対しても高い活性を示すことから、同じような酵素的特性を持つことが示された。最適pHは4.5ｶﾗ5.5を示し、温度安定性は70℃、20分処理で約50％の残存活性を示した。一方、α−グルコシダーゼ�Vと�Wは、マルトースを基質とした際のKm値が可溶性デンプンよりも3−4倍低い値を示し、マルトオリゴ糖に対しては高い活性を示すが、α−グルカンに対してはほとんど活性を示さないことから、同じような酵素的特性を有することが示された。最適pHは4.5−5.5、そして70℃、20分処理では活性が認められなかった。しかしながら、抗α−グルコシダーゼ�V血清は、α−グルコシダーゼ�Vに対してのみ特異的に沈降線を形成した。
kn-abstract=Four molecular forms of α-glucosidase were isolated from spinach seeds by several kinds of chromatography. The molecular masses of α-glucosidases �T,�U,�V,and �W were 78,78,82 and 82kDa by SDS-PAGE, and 62,62,190,and 70kDa by gel filtration, respectively. α-Glucosidases �Tand �U 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 �V and �W 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 �V serum precipitated specifically with α-glucosidase �V.
en-copyright=
kn-copyright=

en-aut-name=SugimotoManabu
en-aut-sei=Sugimoto
en-aut-mei=Manabu
kn-aut-name=杉本学
kn-aut-sei=杉本
kn-aut-mei=学
aut-affil-num=1
ORCID=

en-aut-name=FuruiSatoshi
en-aut-sei=Furui
en-aut-mei=Satoshi
kn-aut-name=古井聡
kn-aut-sei=古井
kn-aut-mei=聡
aut-affil-num=2
ORCID=

en-aut-name=SuzukiYukio
en-aut-sei=Suzuki
en-aut-mei=Yukio
kn-aut-name=鈴木幸雄
kn-aut-sei=鈴木
kn-aut-mei=幸雄
aut-affil-num=3
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学

affil-num=2
en-affil=
kn-affil=岡山大学

affil-num=3
en-affil=
kn-affil=岡山大学
en-keyword=α-Glucosidase
kn-keyword=α-Glucosidase
en-keyword=Spinach
kn-keyword=Spinach
en-keyword=Seed
kn-keyword=Seed
en-keyword=Spinacia oleracea L.
kn-keyword=Spinacia oleracea L.
en-keyword=Molecular form
kn-keyword=Molecular form
END

start-ver=1.4
cd-journal=joma
no-vol=
cd-vols=
no-issue=
article-no=
start-page=
end-page=
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=1994
dt-pub=19940325
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=ヒトIV型コラーゲンα4鎖のcDNAの分離,同定と一部の遺伝子構造の解析
kn-title=cDNA isolation and partial gene structure of the human α 4 (�W) collagen chain
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=
en-copyright=
kn-copyright=

en-aut-name=
en-aut-sei=
en-aut-mei=
kn-aut-name=杉本学
kn-aut-sei=杉本
kn-aut-mei=学
aut-affil-num=1
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学
END