[Dynamics of the blood serum protein fractions in patients with insulinoma]. / Dinamika belkovykh fraktsii syvorotki krovi u bol'nykh s insulinomami.

Gel electrophoresis was used to study the blood serum of 13 patients with insulinomas who showed marked dysproteinemia in the preoperative period. Enucleation of the tumour or resection of the pancreas were performed depending on the location of the tumours. In the immediate postoperative period dysproteinemia became more pronounced, then a tendency to normalization of the protein spectrum occurred. Dysproteinemia was most pronounced at the zone of the starting peak where insulin-binding proteins are located.

[Properties of muscle glycerol-3-phosphate dehydrogenase in rabbits with Brown-Pearce carcinoma]. / Svoistva myshechnoi glitserol-3-fosfatdegidrogenazy krolikov s kartsinomoi Brouna-Pirs.

Specific activity of glycerol-3-phosphate dehydrogenase, estimated in direct and reverse reactions, was decreased, as compared with normal state, without any alterations in the ratio of activities, in muscle homogenates of rabbits with Brown-Pearce carcinoma. The enzymatic activity was decreased by an order of magnitude in homogenates of the tumor as compared with muscle homogenates of the tumor-bearing animals simultaneously with relative stimulation of the reverse reaction. Specific activity of the crystalline enzyme from muscles of tumor-bearing animals was decreased as compared with normal tissues but the ratio of activities was 2-fold increased due to the reverse reaction. In the carcinoma activity of one of the three enzyme fractions, obtained after isoelectrofocusing, was similar to the control values; in the second fraction the ratio of activities was decreased due to inhibition of the direct reaction, the third fraction was inactive. Amino acid composition of crystalline glycerol-3-phosphate dehydrogenase, isolated from tumor-bearing animals, was different in content of 5 amino acids from the enzyme amino acid composition of controls, thus suggesting the structural differences of the proteins from these fractions.

[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.

[Amino acid composition and subunit structure of rabbit muscle aldolase in experimental atherosclerosis]. / Aminokislotnyi sostav i sub"edinichnaia struktura al'dolazy iz myshts krolikov v usloviiakh éksperimental'nogo ateroskleroza.

Under atherosclerosis the fractions corresponding to alpha-subunits are focused at a more alkaline pH than the same fractions in the norm. The curve of the enzymic activity of the fractions with atherosclerosis is higher. beta-subunits of aldolase from muscles of intact rabbits and those with sclerosis are identical in the amino acidic composition. In the enzyme alpha-subunits under conditions of atherosclerosis the content of lysine, serine, glycine, valine gets higher. On the basis of the previous research which reveals peptide having no analogs in the norm in the C-terminal fragment of aldolase molecule an assumption is advanced that under conditions of atherosclerosis the intermediate C-terminal site of the enzyme alpha-chain changes.

[Lipid transport by serum albumin in normal conditions and diseases of the hepatopancreatoduodenal system]. / Transport lipidov syvorotochnym al'buminom v norme i pri zabolevaniiakh gepatopankreatoduodenal'noi zony.

The content of lipids transported by serum albumin was determined in healthy people and in patients suffering from diseases of the hepatopancreatoduodenal zone. The method of gas-liquid chromatography detected 30 fatty acids and the components of steroid nature lipid extracts of albumin. The content of oleic, palmitic, linoleic, stearic and arachidonic acids in the extracts is the highest. Their amount in norm is 75% of all fatty acids. It is shown that bilirubin displaces steroids from the sites of their fixation in albumin. With diseases of the hepatopancreatoduodenal zone serum albumin transports a greater amount of fatty acids with C14-C19 and less amount of those with C20-C25. A constant decrease in the arachidonic acid content is the most typical of the hepatobiliary system diseases.

[Isoelectric fractions of healthy human serum albumin and their ability to bind bilirubin]. / Izoelektricheskie fraktsii syvorotochnogo al'bumina zdorovykh liudei i ikh sposovnost' sviazyvat' 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.