G Iu Azhitskiĭ

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Compositions of borate-polyol buffer solutions were developed, which enabled to produce pH gradients stable to the effect of electric potential in the limits of pH 1.9-4.5, pH 9.6-12.0 and pH 2.0-10.0. These buffers were used for isoelectrofocusing of proteins, low molecular peptides and amino acids.
Albumin from blood serum of healthy persons and from patients with various pathologies and different severity of diseases was characterized using isoelectric focusing in borate-polyol system. In all the pathologies studied a new component occurred, which had an isoelectric point at pH 5.5 and which was not found in fresh albumin preparations isolated from(More)
From 7 to 8 minor fractions were isolated from normal and pathologically altered human blood serum albumin by means of isoelectric focusing in borate-polyol system. As distinct from the whole albumin molecule, these minor fractions contained 12-14% carbohydrates, I-1.2% of which were linked by covalent bonds while the rest of it were absorbed. The fractions(More)
A procedure developed involved isoelectrofocusing in borate-polyol system and thin-layer electrophoresis in polyacrylamide gel gradient containing sodium dodecylsulfate of the products of human blood serum albumin obtained after partial hydrolysis. The first dimension isoelectrofocusing in borate-polyol system allowed to separate peptides with close values(More)
The article deals with the isoelectric spectrum of human serum albumin isolated by electrophoresis in polyacrylamide gel, on agar-agar, by salting out with ammonium sulphate and also by the Cohn method. It is shown that the way of albumin isolation, except the Cohn method, does not affect the quantitative and qualitative characteristics of its isoelectric(More)