Dzheia P P, Kal'venas A A, Toleĭkis A I, Prashkiavichius A K
Biokhimiia. 1986 Jun;51(6):974-9.
The effect of adenylate kinase activity on the rate and efficiency of energy transport from mitochondria to hexokinase was studied in a system containing isolated rabbit heart mitochondria, hexokinase and adenylate kinase at low concentrations of adenine nucleotides. Oxygen consumption by mitochondria and glucose-6-phosphate synthesis by hexokinase were recorded. It was found that with adenylate kinase being active both in mitochondria and in the washing solution, the rate and efficiency of glucose-6-phosphate synthesis considerably increases. The effects of adenylate kinase activity are fully abolished by diadenosine pentaphosphate, an inhibitor of adenylate kinase. The experimental results based on the use of adenylate kinase demonstrate the possibility of increasing the rate and efficiency of energy transfer between two spatially uncoupled biochemical processes in vitro with the aid of an enzymatic system.
在含有分离的兔心脏线粒体、己糖激酶和腺苷酸激酶的体系中，于低浓度腺嘌呤核苷酸条件下，研究了腺苷酸激酶活性对能量从线粒体转运至己糖激酶的速率和效率的影响。记录了线粒体的耗氧量和己糖激酶合成6-磷酸葡萄糖的情况。结果发现，当腺苷酸激酶在线粒体和洗涤液中均有活性时，6-磷酸葡萄糖合成的速率和效率显著增加。腺苷酸激酶抑制剂二磷酸五腺苷可完全消除腺苷酸激酶活性的影响。基于使用腺苷酸激酶的实验结果表明，借助酶系统在体外提高两个空间上不偶联的生化过程之间能量转移的速率和效率是可能的。
