The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
4‐Hydroxyalk‐2‐enals are substrates for glutathione transferase
Abstract
The 4‐hydroxyalk‐2‐enals are established products of lipid peroxidation that are conjugated with intracellular glutathione. Cytosolic glutathione transferases from rat liver were shown to give high specific activities with 4‐hydroxynonenal and 4‐hydroxydecenal. The isoenzyme giving the highest specific activity was glutathione transferase 4‐4. The rate of the spontaneous conjugation reaction is negligible in comparison with the rate calculated for the cellular concentration of the glutathione transferases. It is proposed that a major biological function of the glutathione transferases is to protect the cell against products of oxidative metabolism, such as epoxides, organic hydroperoxides, and 4‐hydroxyalkenals.
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Cites
[51] Assays for differentiation of glutathione S-Transferases
Habig, W. H., & Jakoby, W. B. (1981) · Methods in Enzymology · doi:10.1016/s0076-6879(81)77053-8 · Cited by 2,419
Benedetti, A., Comporti, M., & Esterbauer, H. (1980) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(80)90209-x · Cited by 1,085
Cited by
Interaction of lipid peroxidation products with DNA. A review
Vaca, C. E., Wilhelm, J., & Harms-Ringdahl, M. (1988) · Mutation Research/Reviews in Genetic Toxicology · doi:10.1016/0165-1110(88)90022-x · Cited by 448
Biological interactions of α,β-unsaturated aldehydes
Witz, G. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90137-8 · Cited by 334
Lumjuan, N., Rajatileka, S., Changsom, D., Wicheer, J., Leelapat, P., Prapanthadara, L.-A., Somboon, P., Lycett, G., & Ranson, H. (2011) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2010.12.005 · Cited by 280
Cheng, J.-Z., Sharma, R., Yang, Y., Singhal, S. S., Sharma, A., Saini, M. K., Singh, S. V., Zimniak, P., Awasthi, S., & Awasthi, Y. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106838200 · Cited by 185
Zhang, W., Dai, J., Hou, G., Liu, H., Zheng, S., Wang, X., Lin, Q., Zhang, Y., Lu, M., Gong, Y., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.042 · Cited by 125
Metadata
- Authors
- Ålin, P., Danielson, U. H., & Mannervik, B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1985-01-07
- Volume
- 179
- Issue
- 2
- Pages
- 267-270
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2036338889
- Cited by
- 420
- References
- 2
- FWCI
- 4.96
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ålin, P., Danielson, U. H., & Mannervik, B. (1985). 4‐Hydroxyalk‐2‐enals are substrates for glutathione transferase. FEBS Letters. https://doi.org/10.1016/0014-5793(85)80532-9
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