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Purification and Properties of Rat Liver Microsomal Stearyl Coenzyme A Desaturase
Open accessAbstract
The terminal enzyme of the NADH-dependent stearyl coenzyme A desaturase system has been isolated from rat liver microsomes. This desaturase is a single polypeptide of 53,000 daltons containing 62% nonpolar amino-acid residues and one atom of non-heme iron. The purified protein forms high molecular weight aggregates that can be dispersed by detergent procedures. Desaturase activity requires NADH, stearyl coenzyme A, oxygen, lipid, and the three enzymes, cytochorme b 5 reductase (EC 1.6.2.2), cytochrome b 5 , and desaturase. Cytochrome b 5 is the direct electron donor to the desaturase, which appears to utilize the iron in the oxidation-reduction sequence during desaturation of stearyl coenzyme A.
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Cited by
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Metadata
- Authors
- Strittmatter, P., Spatz, L., Corcoran, D., Rogers, M. J., Setlow, B., & Redline, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1974-11
- Volume
- 71
- Issue
- 11
- Pages
- 4565-4569
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2124728752
- Cited by
- 469
- References
- 0
- FWCI
- 9.22
- Type
- journal article
- Language
- en
- Open access
- green
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- Strittmatter, P., Spatz, L., Corcoran, D., Rogers, M. J., Setlow, B., & Redline, R. (1974). Purification and Properties of Rat Liver Microsomal Stearyl Coenzyme A Desaturase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.71.11.4565
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