Suppression of methemoglobin formation by glutathione in a concentrated hemoglobin solution and in a hemoglobin-vesicle

H. Sakai, S. Takeoka, Y. Seino, E. Tsuchida

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Abstract

The suppression of methemoglobin (metHb) formation by glutathione (GSH) is difficult because GSH is oxidized not only by the reduction of metHb, but also by oxygen to generate active oxygen species, such as superoxide (O2-.) and hydrogen peroxide (H2O2), which contribute to metHb formation. An effective nonenzymatic reduction of metHb was achieved at a high concentration of Hb (40 wt%, 2.48 x 10-2 M subunits (1 M = 1 mol dm-3)) because the reduction of metHb was accelerated, and at a low partial pressure of oxygen (pO2 = 40 Torr (1 Torr = 133.322 Pa)) because the oxidation of GSH was effectively suppressed. Hb-vesicles, which encapsulate concentrated Hb (40 wt%, 2.48 x 10-2 M subunits), transport oxygen in the blood stream at relatively low pO2 (110 Torr in artery and 40 Torr in venous, 58 Torr in average). The rate of metHb formation in Hb-vesicles was effectively decreased from 3.8 x 10-7 to 1.6 x 10-7 Ms-1 by coencapsulating GSH at 58 Torr.

Original languageEnglish
Pages (from-to)1120-1125
Number of pages6
JournalBulletin of the Chemical Society of Japan
Volume67
Issue number4
DOIs
Publication statusPublished - 1994 Jun 29

ASJC Scopus subject areas

  • Chemistry(all)

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