Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Reactive oxygen species do not cause arsine-induced hemoglobin damage

Journal Article · · Journal of Toxicology and Environmental Health
;  [1]
  1. Univ. of Arizona, AZ (United States)

Previous work suggested that arsine- (AsH{sub 3}-) induced hemoglobin (HbO{sub 2}) damage may lead to hemolysis (Hatlelid et al., 1996). The purpose of the work presented here was to determine whether reactive oxygen species are formed by AsH{sub 3} in solution, in hemoglobin solutions, or in intact red blood cells, and, if so, to determine whether these species are responsible for the observed hemoglobin damage. Hydrogen peroxide (H{sub 2}O{sub 2}) was detected in aqueous solutions containing AsH{sub 3} and HbO{sub 2} or AsH{sub 3} alone but not in intact red blood cells or lysates. Additionally, high-activity catalase (19,200 U/ml) or glutathione peroxidase (68 U/ml) added to solutions of HbO{sub 2} and AsH{sub 3} had only a minor protective effect against AsH{sub 3}-induced damage. Further, the differences between the visible spectra of AsH{sub 3}-treated HbO{sub 2} and H{sub 2}O{sub 2}-treated HbO{sub 2} indicate that two different degradative processes occur. The presence of superoxide anion (O{sub 2}{sup {minus}}) was measured by O{sub 2}{sup {minus}} -dependent reduction of nitro blue tetrazolium (NBT). The results were negative for O{sub 2}{sup {minus}}. Exogenous superoxide dismutase (100 {mu}g/ml) did not affect AsH{sub 3}-induced HbO{sub 2} spectral changes, nor did the hydroxyl radical scavengers, mannitol, and DMSO (20mM each). The general antioxidants ascorbate ({le} 10 mM) and glutathione ({le}1 mM) also had no effect. These results indicate that the superoxide anion and the hydroxyl radical (OH) are not involved in the mechanism of AsH{sub 3}-induced HbO{sub 2} damage. The results also indicate that although AsH{sub 3} contributes to H{sub 2}O{sub 2} production in vitro, cellular defenses are adequate to detoxify the amount formed. An alternative mechanism by which an arsenic species is the hemolytic agent is proposed. 16 refs., 4 figs., 2 tabs.

Sponsoring Organization:
USDOE
OSTI ID:
530807
Journal Information:
Journal of Toxicology and Environmental Health, Journal Name: Journal of Toxicology and Environmental Health Journal Issue: 5 Vol. 50; ISSN 0098-4108; ISSN JTEHD6
Country of Publication:
United States
Language:
English

Similar Records

Reactions of arsine with hemoglobin
Journal Article · Thu Feb 08 23:00:00 EST 1996 · Journal of Toxicology and Environmental Health · OSTI ID:426080

Biological responses of human apurinic endonuclease to radiation-induced DNA damage
Conference · Fri Dec 30 23:00:00 EST 1994 · OSTI ID:134861

Oxidation of aqueous polyselenide solutions. A mechanistic pulse radiolysis study
Journal Article · Thu May 04 00:00:00 EDT 2000 · Journal of Physical Chemistry A: Molecules, Spectroscopy, Kinetics, Environment, amp General Theory · OSTI ID:20034421