硫转移酶
互补DNA
胞浆
分子生物学
重组DNA
生物化学
生物
异型生物质的
分子克隆
克隆(编程)
融合蛋白
基因表达
基因
酶
计算机科学
程序设计语言
作者
Saki Takahashi,Yoichi Sakakibara,Emi Mishiro,Haruna Kouriki,Rika Nobe,Katsuhisa Kurogi,Shin Yasuda,Ming‐Cheh Liu,Masahito Suiko
摘要
By searching the mouse EST database, we identified a novel mouse cytosolic sulfotransferase (SULT) cDNA (RIKEN cDNA 2410078J06). Sequence analysis revealed that this new SULT belongs to the cytosolic SULT6 gene family. The recombinant form of this newly identified SULT, designated SULT6B1, was expressed using the pGEX-4T-1 glutathione S-transferase fusion system and purified from transformed BL21 Escherichia coli cells. Purified mouse SULT6B1 exhibited sulfonating activity toward thyroxine and bithionol among a variety of endogenous and xenobiotic compounds tested as substrates. pH optimum of purified mouse SULT6B1 was determined to be 8.0. Tissue-specific expression of mouse and human SULT6B1 was examined by RT–PCR. While human SULT6B1 was specifically expressed in kidney and testis, mouse SULT6B1 was detected in brain, heart, kidney, thymus, lung, liver and testis. Further studies are needed in order to clarify the role of SULT6B1 in the metabolism of thyroxine and possibly some xenobiotics in mouse.
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