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. 1974 Nov;71(11):4565–4569. doi: 10.1073/pnas.71.11.4565

Purification and Properties of Rat Liver Microsomal Stearyl Coenzyme A Desaturase

P Strittmatter 1, L Spatz 1, D Corcoran 1, M J Rogers 1, B Setlow 1, R Redline 1
PMCID: PMC433928  PMID: 4373719

Abstract

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 b5 reductase (EC 1.6.2.2), cytochrome b5, and desaturase. Cytochrome b5 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.

Keywords: fatty acid desaturation, membrane-bound enzymes

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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