Sytnik A I, Chumachenko Iu V, Volovik Z N, Demchenko A P
Ukr Biokhim Zh (1978). 1988 Mar-Apr;60(2):66-72.
The aldolase A binding to the lecithin liposomes (Kd = 2.4 +/- 0.1 X 10(-3) M) has been shown by the fluorescence and tryptophan phosphorescence at the room temperature. The interaction is accompanied by an increase in the phospholipid bilayer microviscosity, and some conformational changes in the hydrophobic part of the enzyme, pronouncing themselves in Trp-147 environment rigidity, decrease. The observation of membrane viscosity vs. incubation time revealed practically instant enzyme-membrane interaction and no gradual incorporation. The accessibility of the NAD-binding domain of aldolase for NADH in the liposome presence remains unaltered.
在室温下，通过荧光和色氨酸磷光已表明醛缩酶A与卵磷脂脂质体结合（解离常数Kd = 2.4±0.1×10⁻³ M）。这种相互作用伴随着磷脂双层微粘度的增加，以及酶疏水部分的一些构象变化，表现为色氨酸-147周围环境刚性降低。对膜粘度与孵育时间的观察表明，酶与膜的相互作用实际上是瞬间发生的，不存在逐渐掺入的情况。在脂质体存在的情况下，醛缩酶的NAD结合结构域对NADH的可及性保持不变。
