Transformation of 17β-estradiol to estrone by unknown wild-type enzyme in commercial arylsulfatase from Helix pomatia

IF 2.8 3区 医学 Q2 BIOCHEMICAL RESEARCH METHODS
Jun Zhang , Ze-hua Liu , Ke-meng Zhao , Zhi Dang , Yun Liu , Yu Liu
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引用次数: 0

Abstract

This work for the first time reported the complete transformation of 17β-estradiol (E2) to estrone (E1) by unknown wild-type enzyme present in the widely used commercial arylsulfatase derived from Helix pomatia. It was found that acetate could effectively inhibit the unknown enzyme with a half inhibitory concentration (IC50) of 140.9 μM, while phosphate and citrate showed no inhibition. Since the buffer solutions with phosphate and citrate have been used in the enzymatic hydrolysis of natural estrogen conjugates for decades, the transformation of E2 to E1 likely occurred during such procedure, inevitably leading to overestimated E1, but underestimated E2. It was further suggested that acetate should be used to prevent this undesirable transformation during the enzymatic hydrolysis of natural estrogen conjugates.

商用芳基硫酸酯酶中的未知野生型酶将 17β-estradiol 转化为雌酮
这项研究首次报道了 17β-estradiol (E2) 与雌酮 (E1) 之间的完全转化过程,这种转化过程是通过从 Helix pomatia 提取的广泛使用的商用芳基硫酸酯酶中的未知野生型酶完成的。研究发现,醋酸盐能有效抑制未知酶,其半抑制浓度(IC50)为 140.9 μM,而磷酸盐和柠檬酸盐没有抑制作用。由于磷酸盐和柠檬酸盐缓冲溶液几十年来一直用于天然雌激素共轭物的酶水解,在此过程中很可能发生 E2 向 E1 的转化,从而不可避免地导致 E1 被高估,而 E2 被低估。还有人建议,在酶水解天然雌激素共轭物的过程中,应使用醋酸盐来防止这种不良转化。
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来源期刊
Journal of Chromatography B
Journal of Chromatography B 医学-分析化学
CiteScore
5.60
自引率
3.30%
发文量
306
审稿时长
44 days
期刊介绍: The Journal of Chromatography B publishes papers on developments in separation science relevant to biology and biomedical research including both fundamental advances and applications. Analytical techniques which may be considered include the various facets of chromatography, electrophoresis and related methods, affinity and immunoaffinity-based methodologies, hyphenated and other multi-dimensional techniques, and microanalytical approaches. The journal also considers articles reporting developments in sample preparation, detection techniques including mass spectrometry, and data handling and analysis. Developments related to preparative separations for the isolation and purification of components of biological systems may be published, including chromatographic and electrophoretic methods, affinity separations, field flow fractionation and other preparative approaches. Applications to the analysis of biological systems and samples will be considered when the analytical science contains a significant element of novelty, e.g. a new approach to the separation of a compound, novel combination of analytical techniques, or significantly improved analytical performance.
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