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. 1979 May 15;180(2):273–279. doi: 10.1042/bj1800273

Re-examination of the subcellular localization of thyroxine 5'-deiodination in rat liver.

D Auf Dem Brinke, R D Hesch, J Köhrle
PMCID: PMC1161050  PMID: 39546

Abstract

We describe the existence of at least two thyroxine 5'-deiodinases in rat liver. They co-fractionate with NADPH-cytochrome c reductase, the marker enzyme for membranes of the endoplasmic reticulum. Subcellular-localization studies of the most active microsomal thyroxine 5'-deiodinase were performed under substrate saturation and at optimal pH 6.8. This enzyme was a Km(app.) of about 3 microM-thyroxine and a Vmax. of about 8 ng of tri-iodothyronine/min per mg of protein. Our study confirms in part the earlier reports of microsomal localization of thyroxine 5'-deiodination. However, this process is not mediated by only a single enzyme.

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Selected References

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