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Arch Biochem Biophys. 2004 Jan 1;421(1):108-14.

Different types of glutathionylation of hemoglobin can exist in intact erythrocytes.

Author information

1
Department of Nutrition and Health Science, Faculty of Human Environmental Science, Fukouka Women's University, 1-1-1 Kasumigaoka, Higashi-ku, Fukuoka 813-8529, Japan. s-mawatari@fwu.ac.jp

Abstract

Glutathionylation of hemoglobin (Hb) was studied by incubation of intact human erythrocytes with 1 mM tert-butylhydroperoxide (tBHP). Electrophoresis of the membranes showed a time dependent increase of membrane-bound Hb alpha chain until 10 min, and immunoblotting study showed that membrane-bound Hb alpha chain reacted with anti-glutathione antibody only after 10 min. Concomitant with the Hb alpha chain, membrane associated actin, spectrin, and glyceraldehyde 3-phosphate dehydrogenase reacted with the antibody. Cytosolic Hb of the control erythrocytes reacted with anti-glutathione antibody. Together with our previous paper, the present study indicates that at least three different types of glutathionylation of Hb can exist in erythrocytes. The first type is a mixed disulfide bond between reduced glutathione (GSH) and normal Hb. The second type is a disulfide bond between the cysteine 93 of metHb beta chain and oxidized glutathione (GSSG), and the third type is a disulfide bond between the other cysteine residues of metHb alpha chain and/or metHb beta chain and GSSG.

PMID:
14678791
[Indexed for MEDLINE]

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