大鼠肝脏中甲状腺素5'-脱碘作用的亚细胞定位的重新检测。
Re-examination of the subcellular localization of thyroxine 5'-deiodination in rat liver.
作者信息
Auf Dem Brinke D, Hesch R D, Köhrle J
出版信息
Biochem J. 1979 May 15;180(2):273-9. doi: 10.1042/bj1800273.
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.
摘要
我们描述了大鼠肝脏中至少存在两种甲状腺素5'-脱碘酶。它们与内质网膜的标记酶NADPH-细胞色素c还原酶共分离。在底物饱和及最适pH 6.8条件下，对活性最高的微粒体甲状腺素5'-脱碘酶进行了亚细胞定位研究。该酶的表观Km约为3 μM甲状腺素，Vmax约为每毫克蛋白质每分钟8 ng三碘甲状腺原氨酸。我们的研究部分证实了早期关于甲状腺素5'-脱碘作用微粒体定位的报道。然而，这一过程并非仅由单一酶介导。
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