Abstract:
: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-aminophenol. 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tomoda A,Yamaguchi J,Kojima H,Amemiya H,Yoneyama Ydoi
10.1016/0014-5793(86)80211-3subject
Has Abstractpub_date
1986-02-03 00:00:00pages
44-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(86)80211-3journal_volume
196pub_type
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