Biomedical subjects
Publications and source records attributed to S E Shnol'.
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In solutions of creatine kinase, actin and lactic dehydrogenase oscillations of SH-groups are revealed by three independent methods using three different reagents AgNO3, PCMB, DTNB. The variations of the SH-group titre remain after denaturation of the individual protein solution portions. In the solutions of predenaturated proteins no titre oscillations are observed. Possible cause of the observed oscillations of SH-groups titre may be reversible SH--SS transformation.
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Computations were carried out of 725 recordings of enzymic activity of equal shares of creatinkinase solution. It has been shown that in the course of macroscopic fluctuations (synchronous in the macrovolume of "conformation fluctuations") a discrete characteristic spectrum of protein solution state resolution degree of the spectrum is deteriorated. Application of statistical spectral analysis to characterization of the properties of protein aqueous solutions is suggested.
A canonic shape of the spectrum of macroscopic fluctuations of enzymic activity in creatinkinase solutions [1] is revealed within wide pH range. With pH decrease (from 10.0 to 6.0) the discreteness and reproducibility of the spectra decreases, at pH 5.0 no canonic spectrum was revealed. The discovered dependence of the spectrum shape on pH illustrates possibilities of spectral analysis of macroscopic fluctuations for characterization of the states of protein aqueous solutions.
When studying enzymic activities in successively chosen portions of solutions of pyruvatekinase, hexokinase, lactatedehydrogenase, alkaline phosphatase, acetylcholinesterase and trypsin fast macroscopic fluctuations were revealed. These fluctuations were found earlier in protein preparations of the actomyosin complex and creatinkinase and described as "conformation fluctuations". Similar macroscopic fluctuations were also revealed when measuring the rate of reaction between ascorbic acid and dichlorphenolindophenol (DCAPI). The spectra of macroscopic fluctuations in solutions of different proteins and ascorbic acid+DCAPI are similar to each other in principle. This gives grounds to consider the ability towards macroscopic fluctuations to be a common property of solutions of different substances.
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