Penetration of 2,4,5-trinitrobenzenesulfonate into human erythrocytes. Consequences for studies on phospholipid asymmetry

Haest, C.W.; Kamp, D.; Deuticke, B.

Biochimica et Biophysica Acta 640(2): 535-543

1981


ISSN/ISBN: 0006-3002
PMID: 7213904
Accession: 006078216

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Abstract
The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 .mu.mol/l cells) at 37% C. Even at 0.degree. C a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway. The disappearance of glutathione probably results from the reaction: 2 GSH + trinitrobenzenesulfonate .fwdarw. GSSG + aminodinitrobenzenesulfonate. The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of Hb which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data.