Chumachenko Iu V, Sytnik A I, Mazhul' V M, Nikol'skaia V P
Ukr Biokhim Zh (1978). 1988 Jul-Aug;60(4):40-6.
The structural peculiarities of rabbit muscle aldolase accompanying enhancement of the aldolase activity in diabetes are described from the data of tryptophan phosphorescence at the room temperature and fluorescence polarization. It is shown that the pathology-concomitant conformational changes occur in both the hydrophobic part and NAD-binding site of the enzyme. The character of the structural changes in the hydrophobic part of the protein in diabetes and an increase in the enzymic activity are similar to that observed in normal aldolase after its interaction with NADH and are believed to be associated with the enhancement of the rigidity in the Trp-147 environment.
根据室温下色氨酸磷光和荧光偏振的数据，描述了糖尿病时伴随醛缩酶活性增强的兔肌肉醛缩酶的结构特性。结果表明，在酶的疏水部分和NAD结合位点均发生了与病理相关的构象变化。糖尿病时蛋白质疏水部分的结构变化特征及酶活性增加与正常醛缩酶与NADH相互作用后观察到的情况相似，被认为与色氨酸-147环境中刚性增强有关。
