@article{oai:ous.repo.nii.ac.jp:00000717,
 author = {愛甲, 博美 and Aikoh, Hiromi},
 journal = {岡山理科大学紀要. A, 自然科学, Bulletin of Okayama University of Science. A, Natural Sciences},
 month = {Mar},
 note = {P(論文), The reduction rate of mercuric ion to metallic mercury by superoxide anion produced by xanthine-xanthine oxidase system increased with increased concentrration of xanthine oxidase in the presence of enough xanthine. The reduction rate of mercuric ion by superoxide anion in the presence of nitroblue tetrazolium (NBT) was proportional to the concentration of NBT. The results suggest that NBT is reduced to diformazan by superoxide anion produced by xanthine-xanthine oxidase system and mercuric ion will be reduced to metallic mercury by diformazan. The reduction rate of mercuric ion by cytochrome C-β-nicotinamide-adenine dinucleotide (NADH) system in the presence of cytochrome C reductase was higher than that of cytochrome C-NADH system in the absence of cytochrome C reductase. On the other hand, the reduction rate of mercuric ion by superoxide anion produced by NADH-phenazine methosulfate (PMS) system increased with increased concentration of PMS.},
 pages = {25--32},
 title = {Reduction of mercuric ion to metallic mercury in vitro by some enzymes},
 volume = {21},
 year = {1986},
 yomi = {アイコウ, ヒロミ}
}