大鼠肝脏碘甲状腺原氨酸5′-单脱碘酶与蛋白二硫异构酶关系的生化研究。

S Sakane, I J Chopra, J Takamatsu, N Ohsawa
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引用次数: 1

摘要

利用合成的与PDI活性位点373-390位氨基酸序列相对应的18个氨基酸肽(LAP475c)和抗LAP475c抗体,研究了I型碘甲状腺原氨酸5′-单去碘酶(5′-MD)与蛋白二硫异构酶(PDI)的关系。Western blot分析显示,抗lap475c抗体对溶解大鼠肝微粒体蛋白(SRLMP)中的57K蛋白具有高度特异性。Anti-LAP475c IgG(1:100稀释)沉淀46%的5′-MD。这些数据表明PDI可能在5'-单脱碘反应中起调节作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Biochemical studies of the relationship between iodothyronine 5'-monodeiodinase and protein disulphide isomerase in rat liver.

The relationship between type I iodothyronine 5'-monodeiodinase (5'-MD) and protein disulphide isomerase (PDI) was investigated by using a synthetic 18-amino acid peptide (LAP475c), which corresponds to the sequence of amino acids at position 373-390 of PDI including its active site, and anti-LAP475c antibody. Western blot analysis revealed that our anti-LAP475c antibody was highly specific for 57K protein in solubilized rat liver microsomal protein (SRLMP) that corresponded to PDI. Anti-LAP475c IgG (1:100 dilution) precipitated 46% of 5'-MD. These data suggest that PDI may play a regulatory role in the 5'-monodeiodination reaction.

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