Nucleotide sequence of rat liver iodothyronine 5'-monodeiodinase (5' MD): its identity with the protein disulfide isomerase.
Nucleotide sequence of rat liver iodothyronine 5'-monodeiodinase (5' MD): its identity with the protein disulfide isomerase.
复制标题
大鼠肝碘甲状腺原氨酸 5-单脱碘酶 (5 MD) 的核苷酸序列:其与蛋白质二硫键异构酶的同一性。
DOI:
10.1016/s0006-291x(88)81282-8
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发表时间:
1988
影响因子:
3.1
通讯作者:
Chopra,IJ
中科院分区:
文献类型:
--
作者:
Boado,RJ;Campbell,DA;Chopra,IJ
We report here the isolation and sequence of a near full length cDNA clone for the 5′MD. Screening of gt11 cDNA library with a32P-labeled partial 5′MD clone (#23) yielded two further clones (#2301 and 2302). Clone 2301 was contained entirely within clone 23 while clone 2302 contained 0.5kb upstream of 5′end and 1.0 kb downstream 3′ end of clone 23. Clone 2302 has an open reading frame of 1,447 nucleotides followed by a stop codon and 584 nucleotides of the untranslated 3′end region. The predicted amino acid sequence showed a 99% and a 95% identity with protein disulfide isomerase (PDI) and the membrane associated thyroid hormone binding protein (MTHBP), respectively. Monoclonal antibodies against human placental PDI (HP13) neutralized the 5′MD and showed only one band in western blot analysis of rat liver solubilized microsomal proteins. The results suggest that clone 2302, MTHBP and PDI may be the same protein and that it represents 5′MD.