M
Mitsuo Miyazawa
Researcher at Kindai University
Publications - 333
Citations - 6720
Mitsuo Miyazawa is an academic researcher from Kindai University. The author has contributed to research in topics: Essential oil & Glomerella cingulata. The author has an hindex of 39, co-authored 333 publications receiving 6151 citations.
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Biologically active components against Drosophila melanogaster from Podophyllum hexandrum.
TL;DR: In the course of screening for novel naturally occurring insecticides from Chinese crude drugs, a dichloromethane extract of Podophyllum hexandrum was found to give an insecticidal activity against larvae of Drosophila melanogaster Meigen.
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Antimutagenic activity of isoflavones from soybean seeds (Glycine max merrill).
TL;DR: Two isoflavones, daidzein and genistein, showed a suppressive effect on umu gene expression of the SOS response in Salmonellatyphimurium TA1535/pSK1002 against the mutagen 3-amino-1, 4-dimethyl-5H-pyrido[4,3b]indole (Trp-P-1), which requires liver metabolizing enzymes.
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Antimutagenic Activity of Gigantol from Dendrobium nobile
TL;DR: A methanol extract from Dendrobium nobile showed a suppressive effect on umu gene expression of the SOS response in Salmonella typhimurium TA1535/pSK1002 against the mutagen 2-(2-furyl)-3-(5-nitro-2)-acrylamide (furylfuramide) as discussed by the authors.
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Moscatilin from Dendrobium nobile, a Naturally Occurring Bibenzyl Compound with Potential Antimutagenic Activity
Mitsuo Miyazawa,Hideo Shimamura,Sei-ichi Nakamura,Wataru Sugiura,Hiroshi Kosaka,Hiromu Kameoka +5 more
TL;DR: In this article, a bibenzyl compound that possesses antimutagenic activity was isolated from the storage stem of Dendrobium nobile and used to suppress the expression of the umu gene following the induction of SOS response in Salmonella typhimurium TA1535/pSK1002.
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Physiological adaptation of the Asian corn borer Ostrinia furnacalis to chemical defenses of its host plant, maize.
TL;DR: In an assay in vitro, homogenate of the digestive tract of O. furnacalis larvae degradation was found to be enzymatic and dependent on a cofactor, UDP-Glucose, suggesting that UDP-glucosyltransferase or other UDP- glucose-dependent enzymes were involved.