Yamazoe Y, Ozawa S, Nagata K, Gong D W, Kato R
Department of Pharmacology, School of Medicine, Keio University, Tokyo, Japan.
Environ Health Perspect. 1994 Oct;102 Suppl 6(Suppl 6):99-103. doi: 10.1289/ehp.94102s699.
An aryl sulfotransferase, whose cDNA was isolated from the rat liver library, was found to catalyze bioactivation of minoxidil through N-O-sulfation and N-sulfation of a carcinogenic heterocyclic amine, IQ, by expression in COS-1 cells. cDNA of a human ortholog also was isolated and characterized as a major minoxidil-activating enzyme in human liver. Another group of aryl sulfotransferases catalyzing O-sulfation of carcinogenic N-hydroxyarylamines was separated from livers of rats and humans. These sulfotransferases have been shown to possess similar functional properties and also to relate immunochemically with each other. Current understanding on the primary structure of these sulfotransferases also is discussed.
从大鼠肝脏文库中分离出一种芳基硫酸转移酶的cDNA,通过在COS-1细胞中表达,发现该酶可通过致癌杂环胺IQ的N-O-硫酸化和N-硫酸化催化米诺地尔的生物活化。人同源物的cDNA也被分离出来,并被鉴定为人类肝脏中主要的米诺地尔活化酶。另一组催化致癌N-羟基芳胺O-硫酸化的芳基硫酸转移酶从大鼠和人类肝脏中分离出来。这些硫酸转移酶已被证明具有相似的功能特性,并且在免疫化学上也相互关联。本文还讨论了目前对这些硫酸转移酶一级结构的认识。