In vitro inhibition of alkaline phosphatase activities from intestine, bone, liver, and kidney by phenobarbital.

Enzyme Pub Date : 1992-01-01 DOI:10.1159/000468804
S Tardivel, H Banide, Z Porembska, Y Dupuis, P Aymard, B Lacour
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引用次数: 5

Abstract

A kinetic study of the inhibition of several alkaline phosphatase (AP isoenzyme activities by phenobarbital was carried out using p-nitrophenylphosphate (10 mM) as a substrate at pH 9.8 in a 300-mM Hepes buffer. AP from bovine kidney, calf intestine, bovine liver, and rat bone was used. Over a phenobarbital concentration range of 20-400 mM, all these isoenzymes were inhibited in an uncompetitive manner with a Ki of 200 mM for intestinal AP, and in a linear mixed-type manner for all the other isoenzymes tested. The Ki values were 10, 40 and 55 mM for kidney, bone and liver AP, respectively. The use of 15 mM carbonate-bicarbonate or 400 mM diethanolamine buffer did not modify the degree of inhibition of intestinal AP activity. Dixon plots of the reciprocal of reaction velocity versus inhibitor concentration either at different substrate concentration or at different DEA concentration indicate uncompetitive inhibition for the intestinal enzyme. This in vitro inhibitory effect of phenobarbital is in contrast to its in vivo stimulating action on AP. However, in the whole animal, the effects of phenobarbital administration probably represent the sum of multiple effects.

苯巴比妥体外抑制肠、骨、肝、肾碱性磷酸酶活性的研究。
在300-mM Hepes缓冲液中,以对硝基苯磷酸(10 mM)为底物,pH为9.8,进行了苯巴比妥抑制几种碱性磷酸酶(AP同功酶)活性的动力学研究。采用牛肾、牛肠、牛肝和大鼠骨的AP。在苯巴比妥20-400 mM的浓度范围内,当Ki值为200 mM时,所有这些同功酶都以非竞争方式被抑制,而所有其他同功酶都以线性混合方式被抑制。肾AP、骨AP和肝AP的Ki值分别为10、40和55 mM。15 mM碳酸氢盐或400 mM二乙醇胺缓冲液的使用并没有改变肠道AP活性的抑制程度。在不同底物浓度或不同DEA浓度下,反应速度与抑制剂浓度的倒数Dixon图显示了对肠道酶的非竞争性抑制。苯巴比妥的这种体外抑制作用与其体内对AP的刺激作用是相反的。然而,在整个动物中,苯巴比妥的作用可能是多种作用的总和。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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