Rabega C, Alexandrescu R, Rabega M
Rev Ig Bacteriol Virusol Parazitol Epidemiol Pneumoftiziol Bacteriol Virusol Parazitol Epidemiol. 1976 Jan-Mar;21(1):37-41.
The interaction of an electromagnetic field with the enzymatic substrate-- the sodium salt of fructose-1,6-disphosphate--induces in the latter a new type of physical transition S leads to S. The enzyme, in this case Saccharomyces cerevisiae aldolase, is able to reveal this new state of the substrate by an increase in its specific activity within well established irradiation times. Each enzyme is characterized by the tm (minimal irradiation time of the substrate) a tau (fixed time period) parameters that delimit the two signals. Purified S. cerevisiae aldolase has tm=5 sec. and tau=20 sec., in contrast to muscle aldolase (represented by class I aldolase) which has tm=15 sec. and tau=30 sec. This may be attributed to the fact that most of the enzymatic systems in S. cerevisiae are made up of several distinct molecular forms, involved in more metabolic pathways than in the animal tissue, therefore with various responses to the phenomenon of perturbation of the substrates.
电磁场与酶促底物——果糖-1,6-二磷酸钠盐——的相互作用会在后者中诱导出一种新型的物理转变S→S。在这种情况下，该酶为酿酒酵母醛缩酶，它能够在既定的辐照时间内通过底物比活性的增加来揭示底物的这种新状态。每种酶都由界定两个信号的tm（底物的最小辐照时间）和tau（固定时间段）参数表征。纯化的酿酒酵母醛缩酶的tm = 5秒，tau = 20秒，相比之下，肌肉醛缩酶（以I类醛缩酶为代表）的tm = 15秒，tau = 30秒。这可能归因于以下事实：酿酒酵母中的大多数酶系统由几种不同的分子形式组成，参与的代谢途径比动物组织中的更多，因此对底物扰动现象有各种不同的反应。
