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Cited by 368

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Permeation of the erythrocyte stroma by superoxide radical

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Lynch, R.E., Fridovich, I.·1978·Journal of Biological Chemistry

Abstract

Superoxide anion, generated by xanthine oxidase within vesicles formed from washed erythrocyte ghosts, crosses the vesicle membrane to reduce cytochrome c in the medium (Lynch, R. E., and Fridovich, I. (1978) J. Biol. Chem, 253, 1838-1845). To determine whether O2- could travel through the membrane in the "channel" for the exchange of stable anions, the effects of two specific inhibitors of anion exchange, 4-acetamido-4'-isothiocyano-2,2' disulfonic acid stilbene (SITS) and 4,4'-diisothiocyano-2,2' disulfonic acid stilbene (DIDS), on the escape of O2- from vesicles were studied. The reduction of external cytochrome c, caused by O2- produced by the enzymic turnover of internal xanthine oxidase, was 85 to 90% inhibited by SITS and DIDS. If SITS impeded the egress of O2- from vesicles, it should enhance the internal effects of O2- and antagonize the inhibition of these effects by external superoxide dismutase. External superoxide dismutase inhibited the lysis of vesicles containing xanthine oxidase. SITS (60 micron) partially reversed this inhibition. It appears that O2- can cross the membrane of the erythrocyte in the anion channel.

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Metadata

Authors
Lynch, R. E., & Fridovich, I.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1978-07
Volume
253
Issue
13
Pages
4697-4699
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1580002784
Cited by
368
References
19
FWCI
2.87
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Permeation of the erythrocyte stroma by superoxide radical. https://app.cochat.ai/papers/10.1016/s0021-9258(17)30446-5
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Lynch, R. E., & Fridovich, I. (1978). Permeation of the erythrocyte stroma by superoxide radical. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)30446-5

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