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The thiosine dye methylene blue (MB) interaction with human serum albumin (HSA) has been studied. MB was revealed to stabilize the native structure of HSA, since the denaturation temperature of the complexes is shifted to higher values in relation to that of the pure protein. It was also revealed that the absorption spectra of the complexes do not change noticeably, while in the fluorescence spectra the maximal intensity of MB decreases with the albumin concentration enhancement. Analysis of the obtained data allows to conclude that the main binding mode of MB to HSA, providing the stabilization of the protein native structure, is the electrostatic mechanism.

In this work, the effect of electromagnetic waves of millimeter diapason (EMW MM) on both melting parameters of serum albumin from human blood and its solution density has been studied. It was shown that the irradiation of albumin solution results in protein denaturation at higher temperatures than in the case of nonirradiated samples, which indicates the increase of albumin packing degree. It was also shown that the enhancement of albumin solution density takes place which indicates the protein packing degree change as well. The obtained data show that the effect of EMW MM does not depend on frequency of these waves, because alterations are revealed at all studied frequencies — 41.8, 48 and 51.8[Formula: see text]GHz.

Abstract. In present work the effect of millimeter waves on both peroxidase total activity and isoenzyme spectrum in wheat seedling cells has been investigated. It is followed from obtained data that the influence of millimeter waves with low intensity on germinating seeds and plant extract invokes the changes of peroxidase isoenzyme spectrum of wheat shoots. At multiple effect of external field when seedlings are cultivated by irradiated water isoenzyme composition changes are observed as well. The enhancement of peroxidase activity is accompanied with isoenzyme number increasing which indicates that at external effects other genes controlling peroxidase synthesis are activated that results in changing of isoenzyme spectrum.

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