岡山医学会Acta Medica Okayama0030-1558901-21978ミトコンドリアのATPase活性に対するカドミウム,ルテニウムレッド及びカルシウムの相互作用251256ENKatashiKenmotsuThe mutual effects of Cd(2+), ruthenium red and Cd(2+) on the rat liver mitochondrial latent ATPase activity were studied and the following results were obtained. (1) The mitochondrial latent ATPase activity was stimulated by Cd(2+), and higher concentration of Cd(2+) added to the reaction mixture showed higher ATPase activity. (2) The ATPase activity induced by Cd(2+) was inhibited by ruthenium red, having the high affinity for the Ca(2+) -binding site of mitochondria. (3) The ATPase activity induced by Cd(2+) was also inhibited by Ca(2+). (4) In conclusion, the site of mitochondria, on which Cd(2+) activates latent ATPase, will be related with the Ca(2+) -binding site of mitochondria.No potential conflict of interest relevant to this article was reported.岡山医学会Acta Medica Okayama0030-1558929-101980金属水銀のカタラーゼによる取り込みに関する研究 第1報 カタラーゼ活性の異なる動物赤血球の金属水銀の取り込みの差異と粗赤血球カタラーゼ液による取り込み9991005ENKatashiKenmotsuThe uptake of metallic mercury was studied using erythrocytes with different catalase activities taken from various kind of animals. The results were: 1) The uptake of metallic mercury by erythrocytes paralleled the activity of catalase in the erythrocytes with and without hydrogen peroxide, suggesting that the erythrocyte catalase activity is related to the uptake of metallic mercury. 2) The uptake of metallic mercury occurred not only with purified human erythrocyte catalase but also with hemolysate. 3) The uptake of metallic mercury by purified human erythrocyte catalase was inhibited by inhibitors of catalase, namely 3-amino-1,2,4-triazole, potassium cyanide and azide. It was concluded that erythrocyte catalase activity has an important role in the uptake of metallic mercury.No potential conflict of interest relevant to this article was reported.岡山医学会Acta Medica Okayama0030-1558939-101981金属水銀のカタラーゼによる取り込みに関する研究 第2報 ラット肝の遊離細胞,ホモジネート,細胞内顆粒,へム蛋白質及び3価の鉄イオンによる金属水銀の取り込みとエチルアルコール及びメチルアルコールの作用835843ENKatashiKenmotsuIn Vitro metallic mercury uptake by rat liver dissociated cells, homogenate, cell components (microbody-rich fraction, mitochondrial fraction and microsomal fraction), heme protein (catalase, cytochrome c, methemoglobin and hematine) and ferric ion were investigated. The effects of ethyl and methyl alcohol on the uptake were also investigated. The following results were obtained. 1) Mercury uptake by rat liver dissociated celld was similar to the uptake by homogenate. 2) Mercury uptake by rat liver homogenate in the presence of hydrogen peroxide was 1.22 times the uptake in the absence of hydrogen peroxide. The uptake by rat liver dissociated cells in the presence of hydrogen peroxide was similar to the uptake in the absence of hydrogen peroxide. 3) Mercury uptake by crystalline catalase, rat liver dissociated cells and homogenate was inhibited by ethtl alcohol and methyl alcohol, though inhibition of catalase activities was not observed. 4) Mercury uptake by rat liver cell components was observed in the order of microbody-rich fraction > microsomal fraction > mitochondrial fraction, and catalase activities were also observed in the order of microbody-rich fraction > microsomal fraction > mitochondrial fraction. Mercury uptake by rat liver cell components was inhibited by potassium cyanide and azide. 5) Cytochrome c, methemoglobin, catalase and ferric ion oxidized metallic mercury in the presence of hydrogen peroxide. In the absence of hydrogen peroxide, methemoglobin and ferric ion oxidized, but catalase and cytochrome c did not oxidize metallic mercury. 6) Hematine did not oxidize metallic mercury with or without hydrogen peroxide. 7) Uptake by ferric ion was inhibited by equimolar addition of EDTA. 8) In the presence of hydrogen peroxide, mercury uptake by catalase was 27,000 times, cytochrome c was 140 times and methemoglobin was 35 times the uptake by ferric ion. Therefore, of heme protein catalase showed the highest mercury uptake.No potential conflict of interest relevant to this article was reported.岡山医学会Acta Medica Okayama0030-1558965-61984金属水銀の取り込みに対するカタラーゼの役割に関する研究 第5報 アカタラセミアマウス及びノーマルマウス呼気中の金属水銀量及び金属水銀曝露時の水銀イオンの臓器分布519525ENKatashiKenmotsuExhalation of metallic mercury from acatalasemic and normal mice intraperitoneally injected with mercuric ion ((203)HgCl(2)) and the mercury uptake by acatalasemic and normal mice exposed to metallic mercury vapor ((203)Hg(0)) were investigated. Exhalation of metallic mercury from acatalasemic mice injected with mercuric ion was higher than that from normal mice. The mercury uptake by normal mice exposed to metallic mercury was higher than that by acatalasemic mice. The liver and brain of acatalasemic mice were higher in the content than those of normal mice. On the other hand, mercury content in heart, lungs, blood and kidneys of acatalasemic mice was lower than in normal mice. The brain/blood concentration ratio of acatalasemic mice was higher than in normal mice. The distribution of mercury in the organs of acatalasemic mice injected with mercuric ion were similar to those of normal mice. Those results indicate that actalase has an important role in the uptake of metallic mercury, and the balance of reduction and oxidation systems influence the metabolism of mercury.No potential conflict of interest relevant to this article was reported.岡山医学会Acta Medica Okayama0030-1558965-61984金属水銀の取り込みに対するカタラーゼの役割に関する研究 第4報 スーパーオキサイドアニオン,NADPH,NADH及びアカタラセミアマウス肝ホモジネートによる水銀イオンの還元511517ENKatashiKenmotsuIn vitro reduction of mercuric ion to metallic mercury by superoxide anion, NADPH, NADH and acatalasemic mouse liver homogenate was investigated. Superoxide anion generated by the xanthine-xanthine oxidase system reduced mercuric ion to metallic mercury in vitro. The reduction rate was inceresed linearly by the increasing concentration of xanthine oxidase. The reduction of mercuric ion by superoxide anion was increased by the addition of cytochrome c and nitro blue tetrazolium. The reduction of mercuric ion was inhibited in the presence of superoxide dismutase and catalase. The rate of reduction of mercuric ion by acatalasemic mouse liver homogenates was higher than that by normal mice liver homogenate. The reduction of mercuric ion by mouse liver homogenate was inhibited by the generation of superoxide anion, but the reduction rate by acatalasemic mouse liver homogenate was higher than that of normal mouse homogenate. NADPH and NADH reduced mercuric ion to metallic mercury. The reduction decreased in the presence of mouse liver homogenate. These results indicate that metabolism of mercury is influenced by the balance of oxidation and reduction systemsNo potential conflict of interest relevant to this article was reported.岡山医学会Acta Medica Okayama0030-1558965-61984金属水銀の取り込みに対するカタラーゼの役割に関する研究 第3報 酵表反応により生成する過酸化水素とカタラーゼによる金属水銀の酸化503509ENKatashiKenmotsuIn vitro oxidation of metallic mercury by catalase and hydrogen peroxide generated by the glucose-glucose oxidase system, D-alanine-D-amino acid oxidase system and xanthine-xanthine oxidase-superoxide dismutase system was investigated. In vitro oxidation of metallic mercury by catalase and hydrogen peroxide generated by the reaction with glucose and glucose oxidase was observed in erythrocytes and crystalline beef liver catalase solution. The uptake depended on the concentration of glucose oxidase and nearly logarithmically increased with the increasing concentration of glucose oxidase. Similar oxidation of metallic mercury was observed in the solution of catalase, D-amino acid oxidase and D-alanine. The uptake also nearly logarithmically increased with increasing concentration of D-amino acid oxidase. In vitro oxidation of metallic mercury by catalase and hydrogen peroxide generated by the reaction system xanthine, xanthine oxidase and superoxide dismutase was observed. Oxidation of metallic mercury similar to that in the xanthine-xanthine oxidase system was observed in the solution of human plasma, hemolysate and erythrocytes containing superoxide dismutase and catalase. These results suggest that hydrogen peroxidase generated by oxidase has an important role in the uptake of metallic mercury vapor.No potential conflict of interest relevant to this article was reported.