四种哺乳动物胆汁酸辅酶A：氨基酸：N-酰基转移酶（BAT）的比较研究

A comparative study of bile acid CoA:amino acid:N-acyltransferase (BAT) from four mammalian species.

Kwakye J B, Johnson M R, Barnes S, Diasio R B

Department of Pharmacology, University of Alabama, Birmingham 35294.

Comp Biochem Physiol B. 1991;100(1):131-6. doi: 10.1016/0305-0491(91)90095-u.

Abstract

Bile acid CoA:amino acid:N-acyltransferase (BAT) was partially purified from dog, human, pig and rat livers. The interspecies variation in substrate specificity and kinetics were determined for glycine and taurine. 2. BAT activity from dog liver formed bile acid conjugates with taurine exclusively, whereas BAT activity from each of the other species formed conjugates with both taurine and glycine. 3. Biliary composition of glycine and taurine bile acid conjugates could partly be accounted for by substrate affinity (Km) and turnover number (Vmax) of BAT activity. 4. A monospecific anti-human BAT polyclonal antibody reacted on Western blot analysis with a 40 kDa band in a 100,000 g supernatant fraction from rat liver. 5. Immunoabsorption chromatography using an anti-human BAT antibody-Sepharose affinity column showed that both the immunoreactive protein band and BAT activity were removed from the 100,000 g supernatant fraction from human and rat livers.

摘要

胆汁酸辅酶A：氨基酸：N-酰基转移酶（BAT）从狗、人、猪和大鼠肝脏中部分纯化出来。测定了甘氨酸和牛磺酸在底物特异性和动力学方面的种间差异。2. 狗肝脏中的BAT活性仅与牛磺酸形成胆汁酸结合物，而其他物种的BAT活性则与牛磺酸和甘氨酸都形成结合物。3. 甘氨酸和牛磺酸胆汁酸结合物的胆汁组成部分可由BAT活性的底物亲和力（Km）和转换数（Vmax）来解释。4. 一种单特异性抗人BAT多克隆抗体在蛋白质免疫印迹分析中与大鼠肝脏100,000 g上清液组分中的一条40 kDa条带发生反应。5. 使用抗人BAT抗体-琼脂糖亲和柱的免疫吸附色谱显示，人及大鼠肝脏100,000 g上清液组分中的免疫反应性蛋白条带和BAT活性均被去除。