功能特性的两个人类sulphotransferase互补编码单胺-和phenol-sulphating形式的苯酚sulphotransferase:底物动力学、热稳定性和inhibitor-sensitivity研究。
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维罗纳人我,朱博格斯W, X,麦克马纳斯我
功能特性的两个人类sulphotransferase互补编码单胺-和phenol-sulphating形式的苯酚sulphotransferase:底物动力学、热稳定性和inhibitor-sensitivity研究。
j . 1994 9月1;302 (Pt 2): 497 - 502。
- PubMed ID
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8093002 (在PubMed]
- 文摘
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本文描述的功能描述两个人类芳基sulphotransferase(所)的互补,HAST1 HAST3,以前由我们从孤立的肝脏和大脑,分别(朱、维罗纳人、桑塞姆和麦克马纳斯(1993)生物化学。Biophys。Commun >, 192年,671 - 676;朱,维罗纳人,伯纳德,桑塞姆和麦克马纳斯(1993)生物化学。Biophys。Commun >, 195年,120 - 127]。似乎这些编码的两种主要形式苯酚sulphotransferase (PST)特征的人体组织细胞溶质,这些被phenolsulphating (P-PST)和monoamine-sulphating (M-PST)苯酚sulphotransferase形式。HAST1和HAST3互补COS-7细胞功能表达和活动特点使用模型基质P-PST和M-PST p-nitrophenol和多巴胺(3 4-dihydroxyphenethylamine)分别。COS-expressed HAST1证明是保持酶的活性在硫酸酯化p-nitrophenol高亲和力(microM 0.6公里),而多巴胺是首选的基质HAST3(9.7公里microM)。多巴胺硫酸HAST1也可以,可以HAST3硫酸盐p-nitrophenol,但是这些反应的公里至少两个数量级大于为基质的首选。 COS-expressed HAST1 and HAST3 displayed inhibition profiles with the ST inhibitor 2,6-dichloro-4-nitrophenol (DCNP), identical with human liver cytosolic P-PST and M-PST activities respectively. Thermal-stability studies with the expressed enzymes showed that HAST1 was considerably more thermostable (TS) than HAST3, which is consistent with P-PST being termed the TS PST and M-PST being termed the thermolabile (TL) PST. Western immunoblot analyses of the expressed PST proteins using an antibody generated to a bacterially expressed rat liver aryl/phenol ST showed that HAST1 and HAST3 migrated as single proteins with different electrophoretic mobilities (32 versus 34 kDa). This is consistent with the differences in electrophoretic mobilities observed for P-PST and M-PST in a variety of tissues reported by other workers. This report on the functional characterization of P-PST and M-PST cDNAs provides important information on the structural as well as functional relationships of human PSTs, which sulphate a vast array of exogenous and endogenous compounds.