pCNBによるメト・ヘモグロビン形成機構に関する研究 : 第2報 pCNBの各種中間体によるin vitroでのメト・ヘモグロビンおよびHeinz小体形成について
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In Report 1, I have reported on the met-hemoglobin and Heinz-body formation in vivo with pCNB and its seven metabolites. It was observed that hydroxylamino-derivative was the strongest agents in the formatian of met-hemoglobin among these metabolites, and it was pointed out that there were possibilities of different mechanisms in different metabolites. I wish to report the results of the case of reactions in vitro to elucidate the mechanisms. 1. Auto-oxidation of metabolites Formerly, W.Heubner ascribed the met-hemoglobin formation of nitro-or amino-compounds to the redox-system of conjugating aminophenol and its imino-quinone, but recently, T.Nakajima et al. reported that only the redox-system of auto-oxidation was not always sufficient to elucidate the facts, and that the oxydase action by perturbed hemoglobin was an essential mechanism in this formation. I have investigated the auto-oxidations of hydroxyl-amino-derivate and others, and the results are shown in Fig.1. As shown in the figure, oxygen-uptake of hydroxylamino-derivatives reached a value near the theoretical value of forming the conjugated azoxybenzene or R-NHO radicals, so I composed p,p'-dichlorazobenzene-N-oxide and tested its ability of met-hemoglobin formation. The results did not support the possibility of the formation of the azoxybenzene system (cf. Fig. 2,3). As to that of the radicals of R-NHO, I cannot discuss it because I could not compose it and estimate its ability of farmation. 2. Auto-oxidation in the case of co-existence with hemoglobin Estimation of the oxygen-uptake of metabolites (pCNB, nitroso, hydroxylamino, amino, aminophenol) in co-existence with diluted blood was made manometrically. As shown in Fig.4, aminophenol and hydroxylamino took oxygen in amounts over their theoretical values. 3. Met-hemoglobin formation in vitro In the above-mentioned experiments, met-hemoglobin formation in vitro occurred in parallel with oxygen uptake. I estimated the values of this met-hemoglobin which are shown in Fig. 5. The order of the amounts formed (aminophenol>hydroxylamino>nitroso, and nil in the cases of nitro and amino) was the same as the order of auto-oxidation of these compounds. The most remarkable difference between the cases, in vivo and in vitro, was that in vivo the strongest was hydroxyalmino but in vitro it was aminophenol. 4. Aerobic and anaerobic met-hemoglobin formations Results of both aerobic and anaerobic formations are shown in Fig. 5. Aminophenol could not form met-hemoglobin without oxygen, but nitroso could. Hydroxylamino could form some quantity of it without oxygen. According to these results, each metabolite is thought to have different mechanisms, and we cannot conclude that the met-hemo globin is formed by such a single mechanism as the nitro or amino compounds being turned into aminophenol and that met-hemoglobin is formed by the redox-system of this aminophenol.
- 社団法人日本産業衛生学会の論文
- 1967-11-20
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