Barańczyk-Kuźma A, Drobisz D, Audus K L, Borchardt R T
Department of Biochemistry, Institute of Biopharmacy, Warsaw Medical School, Poland.
Neurochem Res. 1993 Jul;18(7):783-6. doi: 10.1007/BF00966773.
The substrate specificity and affinity of two forms of phenol sulfotransferase (PST) from Rhesus macaque brain cortex were studied. Catecholamines, their methylated metabolites (normetanephrine, metanephrine) and methylated precursor, alpha-methylDOPA, were examined as substrates for both the cationic (PST I) and the anionic (PST II) forms of the enzyme. Sulfation of hypertensive drugs (phenylephrine, octopamine, metaraminol), hypotensive drugs (alpha-methylDOPA, minoxidil), and related agents without a free hydroxy group on the benzene ring were also studied. Results indicated that both PST forms sulfated alpha-methylDOPA and minoxidil, but only PST II transferred the sulfate group to catecholamines and most of the adrenergic agents examined.
对恒河猴大脑皮层中两种形式的酚磺基转移酶（PST）的底物特异性和亲和力进行了研究。儿茶酚胺、它们的甲基化代谢产物（去甲变肾上腺素、变肾上腺素）以及甲基化前体α-甲基多巴，都作为该酶的阳离子形式（PST I）和阴离子形式（PST II）的底物进行了检测。还研究了降压药（去氧肾上腺素、奥克巴胺、间羟胺）、降压药（α-甲基多巴、米诺地尔）以及苯环上没有游离羟基的相关药物的硫酸化作用。结果表明，两种PST形式都能使α-甲基多巴和米诺地尔硫酸化，但只有PST II能将硫酸基团转移到儿茶酚胺以及所检测的大多数肾上腺素能药物上。
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