Maria Markovich

  • Citations Per Year
Learn More
The possibility of a calorimetric determination of the number of homogeneous independent binding sites on the protein molecule surface is presented, together with the possibility of the determination of interaction heat and association constants for the binding of small molecules to one such site. Thermodynamic characteristics of interaction of 10(More)
Binding of cephazolin, cephalotin and cephamandol to human serum albumin (HSA) was studied by differential scanning calorimetry. It was shown that the binding resulted in an increase in the protein thermostability, while the cooperative character of the biopolymer solution melting was preserved. The constants of association of the above antibiotics with the(More)
The curves of the calorimetric titration of human serum albumin (HSA) with methicillin at different temperatures were plotted. Unlike the widely used serial continuous flow calorimeters, the presented modification of a differential continuous flow microcalorimeter provided its application at wider temperature ranges and higher sensitivity. The possibility(More)
The binding ability of albumin can be increased substantially by treatment with synthetic carbonaceous materials used in medicine [2]. The use of granular hemosorbents and fibrous carbon materials results in the removal of weaklyand stronglyprotein-bound ligands, and correspondingly to an increase in the binding ability of the biopolymer, as shown by(More)
For a study of the reversible binding of natural and semisynthetic penicillins to the albumin fraction of blood serum, various equilibrium physicochemical methods are used. In this work to determine the number of binding sites, the constants of interaction, and the hemodynamics of the association of phenoxymethylpenicillin with human serum albumin (HSA), we(More)
In the first studies [i, 2] of the action of penicillins on microorganisms it was already established that the antibacterial activity of the drug is decreased in the presence of blood serum. Subsequently it was found [3-5] that penicillins interact only with serum albumin, and that all the remaining protein fractions of the serum do not possess the ability(More)
The thermodynamic parameters of human serum albumin (HSA) binding with dicloxacillin, an antibiotic widely used in clinical practice, were determined with the method of differential flow microcalorimetry at 18, 25, 30, 37 and 45 degrees C. The experiments were performed at two ionic strengths: 0.02 and 0.15. Two hypothetic models of interaction in the(More)
Interaction of oxacillin, a semisynthetic penicillin, with human serum albumin (HSA) was studied by means of reaction isothermal and differential scanning microcalorimetry. The antibiotic bound with one primary and two secondary active protein sites. The first bound molecule of the drug had a significant effect on conformation of the biopolymer, which was(More)