Goncharova N Iu, Zelenina E V, Avramova L V
Biokhimiia. 1994 Jun;59(6):826-37.
It was found that the ability of rat skeletal muscle hexokinase isozyme II binding to mitochondrial membranes is realized in full in the presence of Mg2+, glucose and putrescine as adsorption reagent. The hexokinase-membrane complexes obtained through the use of these reagents displayed similar stability as could be judged from their dissociation under identical conditions: either in the presence of KCl used in high concentrations or under the effect of a specific solubilization reagent--glucose-6-phosphate used in physiological concentrations. Within the composition of enzyme-membrane complexes hexokinase had the same kinetic properties which differed, however, from those of the nonbound to mitochondria enzyme. The data obtained are discussed in relation to the hexokinase isozyme II domain responsible for the specific binding of the enzyme to mitochondrial membranes and termed as the "adsorption domain". The availability of this domain is postulated in terms of the concept on the adsorption mechanism of hexokinase isozyme II activity control in skeletal muscles.
研究发现，在存在Mg2+、葡萄糖和腐胺作为吸附剂的情况下，大鼠骨骼肌己糖激酶同工酶II与线粒体膜结合的能力得以充分实现。通过使用这些试剂获得的己糖激酶 - 膜复合物表现出相似的稳定性，这可以从它们在相同条件下的解离情况判断：要么在高浓度KCl存在下，要么在生理浓度的特定增溶试剂——葡萄糖 - 6 - 磷酸的作用下。在酶 - 膜复合物的组成中，己糖激酶具有相同的动力学特性，然而，这与未结合到线粒体的酶的动力学特性不同。结合负责该酶与线粒体膜特异性结合的己糖激酶同工酶II结构域（称为“吸附结构域”）对所获得的数据进行了讨论。根据骨骼肌中己糖激酶同工酶II活性控制的吸附机制概念推测了该结构域的存在。
