Mechanism of o‐aminophenol metabolism in human erythrocytes

FEBS Letters

Tomoda, Akio²  Yamaguchi, Jundo²  Kojima, Hisanori²  Amemiya, Hidemitsu¹  Yoneyama, Yoshimasa² 

[1] Fuji Chemical Industries, 530 Chokeiji, Takaoka, Toyama, Japan;Department of Biochemistry, Kanazawa University School of Medicine, Kanazawa, Ishikawa 920 Japan

关键词: o-Aminophenol metabolism;    2-Aminophenoxazine-3-one;    Erythrocyte;    Hemoglobin;    (Human);   

DOI  :  10.1016/0014-5793(86)80211-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

o-Aminophenol was found to be rapidly metabolized to a brown compound in the presence of purified human oxy- and methemoglobin, coupled with the oxidation and reduction of these hemoglobins by o-amino-phenol. The final product of o-aminophenol was identified as 2-aminophenoxazine-3-one, by using spectrophotometry and HPLC. The metabolism of o-aminophenol was also observed in human erythrocytes. The production rates of 2-aminophenoxazine-3-one in the cells were very fast, but these were strongly decreased by bubbling carbon monoxide into the cell suspension when intracellular hemoglobin was in the ferrous state. The production of 2-aminophenoxazine-3-one from o-aminophenol in the cells was completely suppressed by cyanide and azide when intracellular hemoglobin was in the ferric state. These results suggest that oxy- and methemoglobin are involved in metabolism of o-aminophenol to 2-aminophenoxazine-3-one in human erythrocytes.

【 授权许可】

Unknown