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Biomedical subjects

G Iu Azhitskiĭ

Publications and source records attributed to G Iu Azhitskiĭ.

At least 19 recordsLinked to original sources
PubMed1988

[Qualitative changes in cerebrospinal fluid albumin in cerebral stroke].

Isoelectrical focusing in borate-polyol systems has been used in studies on physico-chemical properties of albumin in the cerebrospinal fluid (CSF) of patients with cerebral stroke. The acute stage of stroke was characterized by an increase in alkaline fractions of CSF albumin with the isoelectrical point (pI) of 5.27-7.4. There is correlation between the levels of alkaline fractions with pI 5.2-7.4 and the severity of patients' status. The method does not help differentiate the nature of stroke but is of a definite prognostic value and characterizes the depth of pathomorphological brain alterations.

Acid-Base Equilibrium↗
PubMed1976

[Human serum albumin: microheterogeneity and hemin-binding ability].

Microheterogeneity of human serum albumin was studied by isoelectric focussing in ampholines and the borax-borate buffer-mannite system within the pH range 4.0--6.0 and by fractional precipitation in 3 M KCl. Albumin was found to have the same degree of heterogeneity in all separating systems. However, during focussing in ampholines microheterogeneity is partially due to the albumin binding with the ampholines. In other systems similar binding was not observed. Studies of the albumin-hemin complex showed that different fractions bind hemin in a different degree, maximal binding being observed within the pH range of 5.0--5.2. Defatting does not affect the distribution of hemin within the fractions of serum albumin.

Chemical Phenomena↗
PubMedDate not supplied

[Isoelectric focusing in a boroborate buffer-mannitol system (BBM)].

The data of the following study of isoelectric focusing in the system 'buffer--nonelectrolyte' are described. The method was shown to be employed for study of proteins, when human serum albumin was used as a model. A standard method and an apparatus device are proposed for the analytical isoelectric focusing of proteins both in the wide (pH 4.00-8.50) and in the limit (PH 4.50-6.00) PH regions. Advantages and limitations of the method are discussed as compared with the method of isoelectric focusing in ampholines.

Borates↗
PubMedDate not supplied

[Isoelectric fractions of healthy human serum albumin and their ability to bind bilirubin].

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 spectrum obtained on ampholines by focusing. Fractions isolated from healthy people have always pI 4.7, 5.1, 5.5, their ratio being different. Albumin and its fractions are identical immunochemically. Dispersion of the fraction content optic rotation, except the fraction with pI 5,1, is the same as in initial albumin. Bilirubin is bound mainly (80%) by the fraction with pI 4.7 and it is absent in the fraction with pI 5.5.

Bilirubin↗
PubMedDate not supplied

[Two-dimensional electrophoresis of the products of limited hydrolysis of human serum albumin using isoelectric focusing in a borate-polyol system].

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 of pI and to increase the procedure sensitivity. The procedure may be recommended for identification of proteins, for estimation of the protein degradation in hydrolysis as well as for studies of peptide maps of albumin under normal and pathological states.

Borates↗
PubMedDate not supplied

[A method of isoelectric focusing in a borate-polyol system with pH gradient of 4.0 to 5.6 in a thin layer of polyacrylamide gel].

A procedure is described for thin-layer polyacrylamide gel isoelectric focusing involving borate-polyol system with gradient pH 4.0-5.6, where 0.5 M H3BO3-Tris was used as an electrode buffer. Riboflavin, TEMED, Tris-borate buffer and glycerol were used in preparation of gradient pH, which was stable and did not alter during the electrophoresis. Blood serum proteins, particularly blood serum albumin, from patients with diabetes were studied using the isoelectric focusing procedure. After isoelectrofocusing of blood serum albumin from patients with diabetes additional minor acid fractions of the protein were detected at pH 4.3-4.6. The procedure of electrophoresis in gradient pH 4.0-5.6 was highly effective and might be used in biochemical laboratories.

Blood Proteins↗