Palaiologos G, Felig P
Yale J Biol Med. 1978 Jan-Feb;51(1):19-26.
Glutamate dehydrogenase (NAD) activity was measured in liver and diaphragm mitochondria from 48 h fasted rats. Kinetic studies were performed with diaphragm enzyme and the effects of L-leu, ADP and L-ala on the K(1)m and V(1)max for NH(4)+, and α-ketoglutarate were evaluated. L-leucine increases by 2-8 fold the V(1)max for all three substrates with no significant changes in the K(1)m. ADP increased by 3-7 fold the V(1)max for all three substrates and the K(1)m for NADH and α-ketoglutarate by 1.5-7.0 fold. L-alanine had no effect on either the V(1)max or the K(1)m of any substrate. The results suggest that muscle has the capacity to form glutamate through the glutamate dehydrogenase reaction and that L-leucine may stimulate this reaction in muscle.
测定了禁食48小时大鼠肝脏和膈肌线粒体中谷氨酸脱氢酶(NAD)的活性。对膈肌酶进行了动力学研究,并评估了L-亮氨酸、ADP和L-丙氨酸对NH₄⁺、α-酮戊二酸的Kₘ和Vₘₐₓ的影响。L-亮氨酸使所有三种底物的Vₘₐₓ增加2至8倍,而Kₘ没有显著变化。ADP使所有三种底物的Vₘₐₓ增加3至7倍,使NADH和α-酮戊二酸的Kₘ增加1.5至7.0倍。L-丙氨酸对任何底物的Vₘₐₓ或Kₘ均无影响。结果表明,肌肉有能力通过谷氨酸脱氢酶反应形成谷氨酸,并且L-亮氨酸可能刺激肌肉中的该反应。