[Localization of disulfide bonds in the alpha 1 acidic glycoprotein molecule and study of their effect on ability of the protein to interact with ethidium bromide]. / Lokalization disul'fidnykh sviazei v molekule kislogo glikoproteina alpha1 i issledovanie ikh vliianiia na sposobnost' belka vzaimodeistvovat' s bromistym étidiem.

alpha 1-Acid glycoprotein (orosomucoid) was purified from the human and murine blood sera using phenol deproteinization. As opposed to the murine protein, the human orosomucoid bound the fluorescent dye ethidium bromide but lost this ability after treatment with beta-mercaptoethanol, which breaks disulfide bonds. Disulfide bonds between the Cys23 and Cys165 residues of the human orosomucoid and between the Cys91 and Cys184 residues of the murine orosomucoid were identified.

[Weight distribution and optical characteristics of soil humic acids fractionated by gel chromatography and electrophoresis]. / Vesovoe raspredeleniie i opticheskiie svoistva pochvennykh guminovykh kislot, fraktsionirovannykh sochetaniem gel'-khromatografii i élektroforeza.

Combination of gel chromatography on Sephadex and polyacrylamide gel electrophoresis was used to obtain molecular weight- and electrophoretic mobility-uniform fractions of humic acids from soil of different types (chernozem, sod-podzol, grey forest, and red soils). Extinction and color (E4/E6) coefficients, as well as weight distribution (%) were studied for all humic acids and their fractions. The fractions differed by the weight distribution (%). Sod-podzol and red soils had twice the amount of high-molecular and half the amount of low molecular HA fractions as compared to chernozem and grey forest soil.

[A new two-stage plan for isolating human alpha1-acidic glycoprotein (orosomucoid). Orosomucoid interacts with ethidium bromide]. / Novaia dvukhstadiinaia skhema vydeleniia chelovecheskogo alpha1- kislogo glikoproteina (orozomukoida). Orozomukoid vzaimodeistvuet s bromistym étidiem.

Human alpha 1-acid glycoprotein (orosomucoid, AGP) was purified to homogeneity by a two-step procedure using phenol and chloroform deproteinization of serum with subsequent preparative electrophoresis on agarose gel. It was obtained 0.15-0.3 mg of protein from 1 ml of serum. Human alpha 1-AGP binds ethidium bromide but not DNA. Neither other human serum proteins nor mice and rat alpha 1-AGP bind ethidium bromide. This property of human orosomucoid depends on its amino acid sequence rather than on the carbohydrate part of the molecule.

[DNA hyperproduction in the blood plasma of animals with experimental diabetes and its compensation using the transplantation of insulin-producing tissue into the anterior chamber]. / Giperproduktsiia DNK v plazme krovi u zhivotnykh s éksperimental'nym diabetom i ee kompensatsiia s pomoshch'iu transplantatsii insulinprodutsiruiushchei tkani v peredniuiu kameru glaza.

Comparative analysis of serum DNA content in healthy rats, rats with experimental alloxan diabetes, and the rats with the diabetes compensated by transplantation of the embryonal pancreas into the anterior chamber of the eye. In the course of diabetes the concentration of free-circulating serum DNA reliably increase 10-12 times, and the compensation of the diabetes returns it to the norm. The revealed relationship may be used for diagnostics of initiation and full compensation of the insulin-dependent diabetes.

[The nucleoprotein fraction of mouse serum in normal and pathological processes]. / Issledovanie nukleoproteinovoi fraktsii syvorotki krovi myshei v norme i pri patologicheskikh protsessakh.

Analysis of the blood serum of healthy and infected with malaria plasmodium mice showed a steep rise in content of linear double-stranded DNA (0.2-0.5 and 2-15 gamma/ml, respectively). Some physico-chemical properties of serum DNA and a DNA-associated glycoprotein (M approximately 40 kDa) are determined.

[Analysis of the trypsin hydrolysate of a 40-kDa protein, found in the nucleoprotein of serum. Identification of it as alpha(1)-acidic glycoprotein (orosomucoid)]. / Analiz produktov tripticheskogo gidrolizata 40-kDa belka, vkhodiashchego v sostav nukleoproteinovoi fraktsii syvorotki krovi. Identifikatsiia ego v kachestve alpha(1)-kislogo glikoproteina (orozomukoida).

From the tryptic hydrolysis of 40-kDa protein from the mouse blood serum thirty-four peptides were isolated by HPLC, of which complete and partial amino acid sequence was established for twenty-eight and six, respectively. On the basis of these data the protein is identified as the blood serum alpha 1-acid glycoprotein.

[Primary structure of the OSCP-protein, conferring the oligomycin sensitivity to the H+-ATPase complex. II. Hydrolysis of OSCP with proteinase from Staphylococcus aureus and reconstruction of the polypeptide chain]. / Pervichnaia struktura OSCP-belka, pridaiushchego mitokhondrial'nomu H+-ATP-aznomu kompleksu chuvstvitel'nost' k oligomitsinu. II. Gidroliz OSCP proteinazoi iz Staphylococcus aureus i rekonstruktsiia polipeptidnoi tsepi belka.

Hydrolysis of OSCP of bovine heart mitochondria by proteinase from Staphylococcus aureus V8 was followed by isolation of all individual peptides by means of gel-filtration and HPLC. Structural analysis of the peptides allowed to arrange BrCN-fragments and to reconstruct the complete amino acid sequence of the protein. Comparative structural analysis revealed existence of a certain homology between OSCP and delta- and b-subunits of the E. coli H+-ATPase, which are necessary for interaction of catalytic and proton-conducting parts of the bacterial enzyme.

[Primary structure of the OSCP protein that confers sensitivity to oligomycin on the mitochondrial H+-ATPase complex. I. Tryptic and cyanogen bromide peptides]. / Pervichnaia struktura OSCP--belka, pridaiushchego mitokhondrial'nomu H+-ATP-aznomu kompleksu chuvstvitel'nost' k oligoitsinu. I. Tripticheskie i bromtsianovye peptidy.

Trypsin and cyanogen bromide were used for cleavage of the OSCP preparations. The peptide mixtures thus formed were separated into individual components by a combination of various chromatographic procedures: gel filtration, ion exchange and paper chromatography, as well as reversed-phase HPLC. As a result, 31 tryptic peptides and 9 out of 10 possible cyanogen bromide peptides were isolated. Determination of the amino acid sequences of these peptide allowed the alignment of cyanogen bromide fragments in the polypeptide chain that shed light on the "architecture" of the protein molecule as a whole. It also afforded the overlappings for tryptic peptides, 16 in the N-terminal and 8 in the C-terminal portions of the molecule.