NEW ASPECTS OF THE INTERACTION OF COPPER (II) WITH SERUM ALBUMIN: VOLTAMMETRIC AND MICROCALORIMETRIC STUDIES.

Structural organization of serum albumins - the most abundant globular proteins in serum plasma - gives rise to their extraordinary binding and functional capacity. Various classes of ligands, including the metal ions can be captured and transported by albumins. Metal binding to human serum albumin, HSA, that is an essential multipurpose target for the modern biomedicine, to its bovine equivalent, BSA, and other mammalian analogs have been extensively explored in the context of metabolism of essential metal ions, like Cu2+.

Notable Stabilization of α-Chymotrypsin by the Protic Ionic Additive, [ch][dhp]: Calorimetric Evidence for a Fine Enthalpy/Entropy Balance.

An impact of 0.5 to 3 M choline dihydrogen phosphate, [ch][dhp], the biotechnologically relevant ionic substance, on the thermal stability of a model globular protein, α-chymotrypsin (α-CT), has been studied exploiting the highly sensitive differential scanning calorimetry (DSC) technique. The notable overall stabilizing effect of 11 ± 2 K regarding the thermal transition (melting) temperature, T m , has been detected.

Laser therapy by noncoherent light field of radiation.

Conducted researches on study of interaction of radiation with blood have shown, that the interaction is the most effective for light with wavelengths in the range of 600-1000 nm that corresponds to the minimum absorption factor of the whole blood. Calculations show, that at interaction of radiation with blood considerably grows effective (electronic) temperature of biological environment, that results in sharp increase of speed of biochemical reactions. The absence of necessity of application of laser radiation coherence in lasertherapy permits to create high efficient noncoherent sources of light on the basis of the GaALAs(Zn) crystals, radiating with two maxima of wavelengths 675 and 900 nm.