STEADY-STATE KINETICS OF RABBIT-INTESTINAL SUCRASE - KINETIC MECHANISM, NA+ ACTIVATION, INHIBITION BY TRIS(HYDROXYMETHYL)AMINOMETHANE AT GLUCOSE SUBSITE
STEADY-STATE KINETICS OF RABBIT-INTESTINAL SUCRASE - KINETIC MECHANISM, NA+ ACTIVATION, INHIBITION BY TRIS(HYDROXYMETHYL)AMINOMETHANE AT GLUCOSE SUBSITE
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DOI：
10.1111/j.1432-1033.1974.tb03255.x
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发表时间：
1974-01-01
期刊：
影响因子：
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通讯作者：
BALTHAZA.AK
中科院分区：
文献类型：
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作者：
SEMENZA, G;BALTHAZA.AK
< jats: p>< jats: list list-type=" explicit-label">< jats: list-item>< jats: p>产物抑制的稳态分析表明，肠道蔗糖酶最可能的动力学机制是乒乓bi-bi（单独水解的有序uni-bi）。< jats: list-item>< jats: p>Na +的激活位点< jats: sup>暂时定位在“葡萄糖”·酶复合物进一步转化之前的水平。< jats: list-item>< jats: p>三羟甲基氨基甲烷与底物竞争葡萄糖亚位点。< jats: list-item>< jats: p>在附录中，描述了用于检测或排除不同或相同动力学类型的抑制剂之间的相互竞争的简单动力学文本。
< jats: p>< jats: list list-type=" explicit-label">< jats: list-item>< jats: p> Steady‐state analysis of product inhibition shows that the most probable kinetic mechanism of intestinal sucrase is ping‐pong bi‐bi (ordered uni‐bi for hydrolysis alone).< jats: list-item>< jats: p> The site of activation by Na< jats: sup>+ was tentatively localized at a level prior to the further transformation of the “glucose”· enzyme complex.< jats: list-item>< jats: p> Tris (hydroxymethyl) aminomethane competes with the substrate for the glucose subsite.< jats: list-item>< jats: p> In the appendix a simple kinetic text is described for detecting or ruling out a mutual competition between inhibitors of different or of identical kinetic type.