[Biosynthesis of immunoglobin G in a cell-free system]. / Issledovanie biosinteza immunoglobulina G v beskletochnoi sisteme.

Optimal conditions are selected to study biosynthesis of proteins by the microsomal cell-free system. It is established that incorporation of the radioactive precursor into anew synthesized proteins by microsomes decreases in a series: the liver, spleen, lymph nodes, bone marrow. It is shown that under malignant growth considerably higher amount of protein with the antigenic properties of immunoglobulin C is synthesized in the spleen of leukemic rats than in other organs of control leukemic animals.

[Physico-chemical properties of IgG characteristic for normal growth]. / Fiziko-khimicheskie svoistva IgG, kharakternogo dlia normal'nogo rosta.

It is shown that IgG typical of the normal growth appears in blood of rats with the regenerating liver and in pregnant ones and its capacity to form complexes with alpha-globulins insoluble in acid medium, isoelectric point and molecular mass are similar to these features in IgG typical of the malignant growth. At the same time hydrophobic properties and energy stability of this protein are close to those of IgG in control animals. The accessibility of ionogenic groups for titration in the studied protein varies like that observed in IgG typical of the malignant growth but is less pronounced. The data obtained evidence for the fact that subpopulations of IgG molecules with similar but not identical properties appear in blood of animals with the normal and malignant growth.

[The effect of growth marker proteins on the ionic permeability of rabbit liver mitochondria]. / Vliianie belkov-markerov rosta na ionnuiu pronitsaemost' mitokhondrii pecheni krolika.

The growth marker proteins from blood serum of new-born rabbits and G-myeloma-bearing people were studied for their effect on ionic permeability of rabbit liver mitochondria. The proteins under study induce an increase in nonspecific ionic permeability and swelling of mitochondria. Thiol compounds, in particular CoA8H (in small concentrations) neutralize the effect of growth marker proteins on the bioenergetic characteristics of mitochondria and lower considerably the protein-induced nonspecific ionic permeability.

[Isolation of immunoglobulin G--marker of normal growth in the blood of the rat]. / Vyiavlenie immunoglobulina G--markera normal'nogo rosta v krovi krys.

The blood of rats with a regenerating liver and of pregnant animals is found to contain a peculiar subfraction of immunoglobulin G (IgG) which is absent in the blood of control animals. A characteristic feature of the protein which permits its detection among other proteins of this class, is its ability to form a complex with serum alpha-globulins insoluble in the acid medium. The complex in composition and conditions of formation differs from that formed by IgG typical of malignant growth. This shows that in blood of animals with normal and malignant growth there appears a subfraction of IgG with similar properties but not identical to it. Isolation of the studied IgG from the formed complex insoluble in the acid medium is suggested as a preparative method for obtaining its subpopulation.

[Structural features of immunoglobulin G from leukemic cattle]. / Strukturnye osobennosti immunoglobulina G krupnogo rogatogo skota, bol'nogo leikozom.

Structural peculiarities of immunoglobulin G (IgG) in cattle with leukemia were studied using the method of dansyl-finger prints and proteolytic fragmentation with pepsin. It is stated that the protein from the blood of leukemic animals differs from the similar IgG subfraction of healthy animals in the amount of peptides: their number is 39 in sick animals, 41--in healthy ones. The studied protein is splitted into three fragments under the effect of pepsin. The molecular mass of F(ab1)2- and Fc1-fragments isolated from the hydrolyzate is 94 and 51 kDa, respectively. Fab-, Fc- and F(ab')2-, Fc'-fragments manifest a complete antigenic identity. The antibody activity is inherent only in the F(ab')2-fragment; it reacts positively in the precipitation test together with monospecific antiserum against IgG, typical of the malignant growth. This confirms a supposition that structural peculiarities of the protein typical of the malignant growth and isolated from the blood of cattle with leukemia depend on changes in the protein Fab-fragment.

[Factors affecting activation of glycolysis by immunoglobulin G]. / Izuchenie faktorov, vliiaiushchikh na aktivatsiiu glikoliza immunoglobulinom G.

Immunoglobulin G characteristic of malignant growth is studied for its effect on glycolysis in a dialyzed enzymic preparation from the rabbit muscles. A peptide-nature compound participating in immunoglobulin G activation of glycolysis is shown to transfer to dialysate in the process of the enzyme dialysis. The activation may involve cAMP, ADP, NADH.

[Isolation and characteristics of immune complexes circulating in the serum of acute leukemia patients]. / Vydelenie i kharakteristika immunnykh kompleksov, tsirkuliruiushchikh v syvorotke krovi bol'nykh ostrym leikozom.

Immunoglobulin G-containing immune complexes are obtained from blood serum of patients with acute leukemia by the method which includes precipitation using polyethylene glycol-6000, Sephadex G-200 gel filtration and protein A-sepharose affinity chromatography (pH 8.5). Immunologically active antibodies and antigens of complexes are isolated by Sephadex G-200 gel chromatography under conditions of dissociation (the sodium-citrate buffer, pH 7.5, 9 M urea). The immune complexes with the antigens and antibodies isolated from them are partially characterized using disc-immunoelectrophoresis, isoelectrofocusing and immune-isoelectrofocusing.

[Effect of protein-markers of growth on oxidative phosphorylation in mitochondria]. / Vliianie belkov-markerov rosta na okislitel'noe fosforilirovanie v mitokhondriiakh.

Growth marker proteins (GMP) were studied for their effect on oxidative phosphorylation in the heart and liver mitochondria of rabbits. It is shown that GMP decrease a respiratory control (RC) coefficient, P/O coefficient, inhibit respiration of the mitochondria in metabolic states 3, 5 and activates it in state 4. The nature of the oxidation substrates (FAD- and NAD-dependent succinic and pyruvic acids, respectively) does not influence the GMP effect manifestation. It is supposed that GMP disturb the structural and functional integrity of the mitochondria. Variations in bioenergetic parameters of the heart and liver mitochondria in organisms with active growth foci as well as of mitochondria incubated with GMP, are unidirectional. Cytochrome c, coenzyme A (Co ASH) and other thyol compounds (cystein, dithiotreitol, glutathione--GSH) remove the GMP action.

[Carbohydrate component of immunoglobulin G in cattle suffering from leukosis]. / Izuchenie uglevodnogo komponenta immunoglobulina G krupnogo rogatogo skota, bol'nogo leikozom.

No essential differences are found in the composition and total amount of carbohydrates in the studied preparations of the immunoglobulin G subfraction in cattle suffering from leucosis and of the immunoglobulin G subfraction, identical in evolution, in healthy animals. It is shown that the main mass of carbohydrates is connected with Fc-fragment and heavy chains of the protein under study.

[Physicochemical and immunochemical properties of heavy chains of immunoglobulin G typical of malignant growth]. / Fiziko-khimicheskie i immunokhimicheskie osobennosti tiazhelykh tsepei immunoglobulina G, kharakterno dlia zlokachestvennogo rosta.

Molecular weight of heavy chains of immunoglobulin G typical of cancer is studied immunoglobulin and may be responsible for manifestation of certain anomalous acid and peptide composition of this protein heavy chains as compared with immunoglobulin G in blood serum of healthy people. Immunochemical methods helped detecting an antigenic determinant (or determinants) which is arranged in the heavy chains of the studied immunoglobulin and may be responsible for manifestation of certain anomalous properties of cancer-typical immunoglobulin G molecules. A set of bromo-cyanogenic fragments differing from the spectrum of these fragments in the heavy chains of normal immunoglobulin G is formed following a specific chemical effect of bromo-cyanogen on the heavy chains of immunoglobulin G typical of cancer. Essential differences are found in dancyl-fingerprints of the heavy chains of the compared proteins. Everything mentioned is a result of changes in the primary structure of the heavy chains of immunoglobulin G typical of cancer.

[Potentiometric studies of ionogenic groups of immunoglobulin G characteristic of malignant growth]. / Potentsiometricheskoe issledovanie ionogennykh grupp immunoglobulina G, kharakternogo dlia zlokachestvennogo rosta.

Application of the method of potentiometric acid-base titration for studying the character of available for titration ionogenic groups of immunoglobulin G characteristic of malignant growth and immunoglobulin G isolated from the health people blood serum made it possible to detect some differences evidencing for different conformation of the molecules of the proteins under study.

[Kinetics of production of slightly soluble aggregates of immunoglobulin G characteristic of malignant growth]. / Kinetika obrazovaniia malorastvorimykh agregatov immunoglobulina G, kharakternogo dlia zlokachestvennogo rosta.

Studies in kinetics of production of slightly soluble aggregates of immunoglobulin G characteristic of malignant growth with serum alpha-globulins under the effect of the acid medium on the sera of cancer patients resulted in establishing that this process is subjected to the equation first order reaction. The analysis of the kinetic curves showed that immunoglobulin G characteristic of malignant growth is available in blood of the patients at all the stages of the tumour development.

[Features of the biosynthesis of immunoglobulin G peculiar to the growth process]. / Osobennosti biosinteza immunoglobulina G, kharskternogo dlia protsessov rosta.

It is established that with partial hepatectomy, Shvets leukosis and hepatoma RS-1 the biosynthesis intensity of rat blood serum proteins producing aggregates in the acid medium is considerably higher than that of other serum proteins, the incorporation of the radioactive precursor into immunoglobulin G peculiar to intensive normal and malignant growth being particularly intensive. During liver regeneration as well as in malignant growth specific radioactivity of immunoglobulin G peculiar to the growth processes is three and five times, respectively, as high as this value for blood serum soluble proteins and proteins of alpha-globulin fractions.

[Peculiarities of hydrophobic structure of immunoglobulin G peculiar to malignant growth]. / Osobennosti gidrofobnoi struktury immunoglobulina G, kharakternogo dlia zlokachestvennogo rosta.

Application of the refractometric method for estimating intramolecular sorption of hydrocarbon by proteins permitted detecting some differences in the hydrophobic structure of immunoglobulin G peculiar to the malignant growth and of immunoglobin G of the healthy organism. An increase in the specific hydrophobic capacity of immunoglobulin G peculiar to the malignant growth due to large hydrophobic regions makes it possible to conclude that this protein globular packing is less compact and looser.

[Role of acid anion in formation of low-soluble aggregates of immunoglobulin G characteristic of malignant growth]. / Rol' aniona kisloty v obrazovanii malorastvorimykh agregatov immunoglobulina G, kharadternogo dlia zlokachestvennogo rosta.

The acid medium favour the formation of low-soluble aggregates in the cancer patient blood serum. An anion of the acid utilized for creation of the aggregate-forming medium is involved into composition of the agregates. The elementary quantitative analysis of such aggregates showed that the amount of the incorporating anion is in inverse dependence on its affinity for proteins. The anion is established to participate at the stage of the low-soluble complex formation. A schematic model is suggested for low-soluble aggregates formed in the cancer patient blood cerum under the effect of the acid medium.

[Composition and properties of immunoglobulin G in cattle with lymphatic leukemia]. / Sostav i svoistva immunoglobulina G krupnogo rogatogo skota pri limfoleikoze.

The data are presented concerning the qualitative changes in cattle immunoglobulin G with lymphoid leukosis. Protein peculiar to cattle leucosis is shown to be an immunoglobulin G subfraction which is washed out of the DEAE-cellulose column by 0.1 M of NaCl. Its molecular mass is 130,000 Daltons. The data of immunoelectrophoresis and ultracentrifugation show that it is homogeneous. The protein sedimentation constant is 7.2 S. The electrophoretic mobility is 0.18-0.19 of bull albumin mobility. The amino acid analysis of this protein shows that the content of methionine in it is more than 20% lower. This evidences for its similarity to protein characteristic of myeloma and Shvets leukosis in rats. This manifests similarly of proteins peculiar to different forms of malignant growth. This protein has common antigenic determinants with the protein peculiar to human malignant growth.

[Physicochemical and immunochemical properties of submolecular structures of immunoglobulin G characteristic of cancer]. / Fiziko-khimicheskie i immunokhimicheskie svoistva submolekuliarnykh struktur immunoglobulina G, kharakternogo dlia raka.

Studies in physicochemical and immunochemical properties of polipeptide chains fragments of immunoglobulin G malignant growth permitted detecting the location site for a specific determinant which adds a unique feature to the whole molecule of immunoglobulin G. The specific antigenic determinant is defined by a group of amino acids located in the heavy chain site corresponding to Fd-fragment. During papain and trypsin hydrolysis of specific immunoglobulin G obtained from different patients the formed sets of fragments and peptides are different. This testifies to the fact that the immunoglobulin under study may belong to any of four subclasses of immunoglobulin G, that is confirmed by the immunochemical analysis with application of monospecific antisera against certain subclasses of immunoglobulin G.