大鼠肝脏雌激素硫酸酯酶和芳基硫酸酯酶C活性的研究。
Studies on the oestrogen sulphatase and arylsulphatase C activities of rat liver.
作者信息
Dolly J O, Dodgson K S, Rose F A
出版信息
Biochem J. 1972 Jun;128(2):337-45. doi: 10.1042/bj1280337.
Abstract
Detailed studies on the hydrolysis of p-acetylphenyl sulphate and oestrone sulphate by rat liver preparations strongly indicate that arylsulphatase C and oestrogen sulphatase are the same enzyme. Liver is the richest source of both enzymes, which have identical intracellular distributions, being localized mainly in the microsomal fraction. Low oestrogen sulphatase and arylsulphatase C activities were present in foetal liver and these increased at a similar rate after birth. The activities of the enzymes in an ethionine-induced hepatoma were similarly low. Results of heat inactivation, mixed-substrate and competitive-inhibition experiments employing liver microsomal fractions were also consistent with one enzyme being involved. Oestradiol-17beta 3-sulphate was also hydrolysed by microsomal preparations and activity towards both this substrate and oestrone sulphate was inhibited by oestrone and oestradiol-17beta. The physiological significance of this inhibition is discussed.
摘要
对大鼠肝脏制剂水解对乙酰苯基硫酸酯和硫酸雌酮的详细研究有力地表明，芳基硫酸酯酶C和雌激素硫酸酯酶是同一种酶。肝脏是这两种酶最丰富的来源，它们在细胞内的分布相同，主要定位于微粒体部分。胎肝中雌激素硫酸酯酶和芳基硫酸酯酶C的活性较低，出生后以相似的速率增加。乙硫氨酸诱导的肝癌中这些酶的活性同样较低。使用肝脏微粒体部分进行的热失活、混合底物和竞争性抑制实验的结果也与涉及一种酶一致。微粒体制剂也能水解17β-雌二醇3-硫酸酯，雌酮和17β-雌二醇对该底物和硫酸雌酮的活性均有抑制作用。讨论了这种抑制作用的生理意义。
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