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
Open accessAbstract
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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Cites
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931
The Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44679-6 · Cited by 1,174
Self-citationFree Radicals and Inflammation: Protection of Synovial Fluid by Superoxide Dismutase
McCord, J. M. (1974) · Science · doi:10.1126/science.185.4150.529 · Cited by 1,108
Cabantchik, Z. I., & Rothstein, A. (1974) · The Journal of Membrane Biology · doi:10.1007/bf01870088 · Cited by 732
Johnston, R. B., Keele, B. B., Misra, H. P., Lehmeyer, J. E., Webb, L. S., Baehner, R. L., & RaJagopalan, K. V. (1975) · Journal of Clinical Investigation · doi:10.1172/jci108055 · Cited by 704
THE ENZYMATIC IODINATION OF THE RED CELL MEMBRANE
Hubbard, A. L., & Cohn, Z. A. (1972) · The Journal of Cell Biology · doi:10.1083/jcb.55.2.390 · Cited by 701
Cabantchik, Z. I., & Rothstein, A. (1972) · The Journal of Membrane Biology · doi:10.1007/bf01867863 · Cited by 533
A major protein which spans the human erythrocyte membrane
Bretscher, M. S. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90055-6 · Cited by 323
Effects of Superoxide on the Erythrocyte Membrane
Lynch, R. E., & Fridovich, I. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62328-8 · Cited by 261
Self-citationSuperoxide production by phagocytic leukocytes.
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Cited by
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029
[1] Role of free radicals and catalytic metal ions in human disease: An overview
Halliwell, B., & Gutteridge, J. M. C. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)86093-b · Cited by 4,994
Skeletal muscle fatigue: cellular mechanisms
Allen, D. G., Lamb, G. D., & Westerblad, H. (2008) · Physiological Reviews · doi:10.1152/physrev.00015.2007 · Cited by 2,495
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Halliwell, B., & Whiteman, M. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705776 · Cited by 2,238
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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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