[Interaction between bee venom melittin and human blood albumin]. / Vzaimodeistvie melittina pchelinogo iada s al'buminom krovi cheloveka.

It is shown that bee venom melittin interacts with human blood albumin at pH 8.0-8.5 in the presence of NaCl (concentration over 0.1%) and forms a precipitating complex (MA), the albumin/melittin ratio being 1:12 for the monomer melittin. With a decrease of pH down to 5.3 and salt concentration below the limit mentioned, the precipitate is destroyed. The complex is soluble in the distilled water. Conditions for carrying the precipitation reaction between albumin and melittin in agarose gel are chosen. The titration method has been used to determine that melittin is bound up with albumin in the molar ratio (10-12):1 for monomeric melittin or 3:1 for tetrameric melittin.

[Effect of various specific agents on the heat stability of human serum albumin]. / Vliianie razlichnykh spetsificheskikh agentov na termostabil'nost' syvorotochnogo al'bumina cheloveka.

Effect of lipoic acid, 5,5-dithiobis-2-nitrobenzoic acid, monoiodoacetic acid and cystine on thermal stability of human serum albumin was studied by differential scanning calorimetry and electrophoretic methods. Quantitative estimation of the protective effect of these reagents on resistance of 5% solutions of albumin to the temperature influence was studied. It is concluded that all the compounds used protect albumin from polymerization at heating.

[Development of a highly efficient method for separating bee venom components]. / Razrabotka vysokoéffektivnogo metoda razdeleniia komponentov pchelinogo iada.

Factors preventing complete separation of melittin and phospholipase A2 under fractionation of the bee venom were studied. The methods of electrophoresis in PAAG, gel-filtration, ion-exchange and reverse-phase chromatography were used to show that the intermolecular interactions of suppositionally hydrophobic character prevent from complete separation of melittin and phospholipase A2. Conditions and methods are chosen which permit isolating melittin and phospholipase in a pure form.

[Qualitative changes in cerebrospinal fluid albumin in cerebral stroke]. / Kachestvennye izmeneniia al'bumina likvora pri mozgovom insul'te.

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.

[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]. / Metodika izoélektricheskogo fokusirovaniia v borat-poliol'noi sisteme v gradiente pH ot 4,0 do 5,6 v tonkom cloe PAAG.

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.

[Two-dimensional electrophoresis of the products of limited hydrolysis of human serum albumin using isoelectric focusing in a borate-polyol system]. / Dvukhmernyi élektroforez produktov ogranichennogo gidroliza syvorotochnogo al'bumina cheloveka s ispol'zovaniem izoélektricheskogo fokusirovaniia v borat-poliol'noi sisteme.

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.

[Thiol-disulfide metabolism as a mechanism in the formation of albumin minor fractions with pI 5.2-7.4 in various pathologic states]. / Tiol-disul'fidnyi obmen kak mekhanizm obrazovaniia minornykh fraktsii al'bumina s pI 5,2-7,4 pri patologiiakh.

The mechanism of formation of minor isoelectric fractions of albumin with pI 5.2-7.4 which arise in the blood channel with pathologies is studied. This phenomenon is nonspecific for any definite type of the disease and is possibly a result of the disease gravity. The mechanism of thiol-disulphide metabolism is shown to underlie the appearance of isoelectric fractions of albumin with pI 5.2-7.4. The fractions possess a lower ability to bind the bromo-phenol blue dye and a higher ability to bind penicillin.

[Isolation and purification of lactoperoxidase from cow's milk]. / Vydelenie i ochistka laktoperoksidazy iz korov'ego moloka.

A procedure is described for isolation and purification of lactoperoxidase from cow milk. The procedure involved the following steps: isolation of casein from milk, sorption of lactoperoxidase on CM-Sephadex, concentration of the eluate using ultrafiltration, salting out with ammonium sulfate; isoelectric focusing was carried out in the borate-polyol system. Highly purified, active preparation of lactoperoxidase was obtained within a relatively short period by means of the procedure, where the available reagents were used.

[Transient minor fractions of human serum albumin: physico-chemical properties]. / Tranzitornye minornye fraktsii syvorotochnogo al'bumina cheloveka: fiziko-khimicheskie svoistva.

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 included a number of amides, amount of which was gradually elevated with an increase in the isoelectric point. As shown by circular dichroism studies content of alpha-spirals decreased from 20% to 5% in the proteins, depending on the pI value. Spontaneous deamidation was noted during storage. Normally the content of these proteins constituted from 3% to 4%; in liver cirrhosis it might increase up to 50%.

[Isoelectric spectra of human serum albumin in healthy subjects and in ischemic heart disease]. / Izoélektricheskie spektry al'bumina syvorotki krovi cheloveka v norme i pri ishemicheskoi bolezni serdtsa.

Isoelectric spectra of serum albumins isolated from blood of patients with heart ischemia were studied using isoelectric focusing in borate-polyolic systems in a polyacrylamide gel. In patients with heart ischemia the amount of fractions with pI 4.3-4.9 and 5.2-7.4 is found to increase with a simultaneous decrease in the fraction with pI 4.9-5.2 as compared with these indices in healthy people from the control group. Especially pronounced changes in isoelectrophoregrams were observed for blood albumins of patients with transmural myocardium infraction.

[Isolation and use of stable borate-polyol pH gradients in the range of 1.9-12.0 for isoelectric focusing of proteins and low-molecular compounds]. / Poluchenie i ispol'zovanie stabil'nykh borat-poliol'nykh gradientov pH v diapazone 1,9-12,0 dlia izoélektricheskogo fokusirovaniia belkov i nizkomolekuliarnykh soedinenii.

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.

[Characteristics of isoelectric fractions of human serum albumin]. / Kharakteristika izoelektricheskikh fraktsii syvorotochnogo al'bumina cheloveka.

Amino acidic composition, dispersion of optic rotation, differential temperature-perturbation spectra, molecular weight and terminal amino acids are studied for certain isoelectric fractions of human serum albumin obtained by means of isoelectric focusing in the borate-polyol system. The isolated three isoelectric fractions with pI 4.7, 4.9 and 5.1 revealed no significant differences in the composition of amino acids. They also did not differ in molecular weight and N- and C-terminal amino acids. However certain differences in the conformation and number of perturbed thyrosils are detected by means of spectral methods.

[Stable borate-polyol pH-gradients and isofocusing of proteins in the range of pH 3.0-9.0]. / Stabil'nye borat-poliol'nye pH-gradienty i izofokusirovanie belkov v diapazone pH 3.0-9.0.

Methods are developed for obtaining pH-gradients stable to the electric current effect in borate-polyol systems which were used for the isofocusing of different proteins. The isofocusing within the range of pH 3.0-9.0 is shown to be possible.

[Isolation and purification of an unspecific component from human serum albumin, typical for pathology]. / Vydelenie i ochistka nespetsificheskogo komponenta syvorotochnogo al bumina cheloveka, kharakternogo dlia patologii.

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 healthy persons. This fraction was isolated and purified. Its isoelectric point was near pH 4.5-4.6 in isoelectrofocusing with ampholines. The divergences were due to complex formation of albumin with ampholines. The modified protein corresponded immunochemically to the human blood serum albumin, did not contain polymers, had a decreased amount of alpha-helix structures as shown by dispersion of optic rotation and its molecular mass was similar to the mass of native albumin.