Mechanism of o-aminophenol metabolism in human erythrocytes.

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 Lett

journal_title

FEBS letters

authors

Tomoda A,Yamaguchi J,Kojima H,Amemiya H,Yoneyama Y

doi

10.1016/0014-5793(86)80211-3

subject

Has Abstract

pub_date

1986-02-03 00:00:00

pages

44-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80211-3

journal_volume

196

pub_type

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