[An immunochemical study of the interaction of human trophoblastic beta-glycoprotein with steroid and sex hormones]. / Immunokhimicheskoe izuchenie vzaimodeistviia trofoblasticheskogo beta-glikoproteina cheloveka s steroidnymi i polovymi gormonami.

Human trophoblastic beta-glycoprotein (TBG) was subjected to immunoelectrophoresis with intermediate gel containing hormones. We have observed TBG binding either with cyclopentaneperhydrophenanthrene derivatives (cholesterol, testosterone, progesterone, estradiol, estrone) or their synthetic analogs (sinestrol, diethylstilbestrol). TGB showed markedly higher affinity to estrogens than to other hormones.

[Comparative physico-chemical characteristics of trophoblastic beta-1 glycoprotein preparations isolated from retroplacental blood]. / Sravnitel'naia fiziko-khimicheskaia kharakteristika preparatov trofoblasticheskogo beta1-glikoproteina, vydelennykh iz retroplatsentarnoi krovi.

Trophoblastic beta 1-glycoprotein preparations (TBG-1, TBG-2) isolated by different methods preserve their physicochemical and immunochemical properties. According to the data of disk-electrophoresis and densitometry TBG-1 preparation obtained using two-stage method is highly purified and protein yield is about 20%, while TBG-2 isolated by multi-stage method has a small number of admixture proteins.

[The cellular localization of the fertility alpha 2-microglobulin in tumors of the reproductive system]. / Kletochnaia lokalizatsiia al'fa-2-mikroglobulina fertil'nosti v opukholiakh reproduktivnoi sistemy.

Seventy-five samples of human tumors were examined immunohistochemically for fertility alpha-2-microglobulin also known as progesterone-associated protein of the endometrium. The protein was detected in 35.7% (5 of 14) endometrial cancer samples and in 20% (2 of 10) of ovarian malignancies. Tumors of the stomach, colon, breast, lung and some other sites failed to reveal the antigen with the exception of a single case of pulmonary adenocarcinoma which showed the ectopic expression of the protein. Fertility alpha-2-microglobulin is stage-specific tissue marker of the endometrium. It is expressed at the final stage of cell differentiation and is partially lost in cancer.

[The hydrophobic properties of beta-glycoprotein from the blood serum of pregnant rats]. / Gidrofobnye svoistva beta-glikoproteina syvorotki krovi beremennykh krys.

During immunoelectrophoresis in the presence of tween-80, triton X-100 and ammonium sulfate blood serum beta-glycoprotein of pregnant rats migrated along with beta-globulins as a main single band; its minor components in zones of alpha- and gamma-globulins were not detected. beta-glycoprotein was completely absorbed by phenyl sepharose in the absence of ligand as well as when the spacer arm for phenyl group was short. When the phenyl group was linked with the template through a long spacer arm, three froms of beta-glycoprotein with different immunoelectrophoretic mobility were detected after absorbtion with phenyl sepharose. Hence, beta-glycoprotein is hydrophobic and is represented by alpha-, beta- and gamma-forms in blood plasma of pregnant rats.

[Immunochemical analysis of the interaction of the fertility alpha 2-microglobulin with steroid sex hormones]. / Immunokhimicheskii analiz vzaimodeistviia al'fa 2-mikroglobulina fertil'nosti so steroidnymi polovymi gormonami.

The interaction between the fertility alpha 2-microglobulin and steroid sex hormones (estrone, estriol, estradiol, progesterone, testosterone) was studied by the use of cross immunoelectrophoresis with intermediate gels. alpha 2-microglobulin was shown to bind to the above hormones, its affinity to testosterone being the highest. The ability of alpha 2-microglobulin to bind to steroid hormones can be used for its isolation by affinity chromatography with immobilized steroid hormones.

[Immunochemical analysis of lectin acceptors in the structure of the fertility alpha 2-microglobulin]. / Immunokhimicheskii analiz aktseptorov k lektinam v strukture al'fa 2-mikroglobulina fertil'nosti.

Fertility alpha 2-microglobulin reacts with 3 out of 8 lectins, which possess affinity to monosaccharides (glucose and mannose) and acetylamino sugar. The affinity is most marked to concanavalin A and is considerably weaker to Pisum sativum and Vicia faba lectins, whereas the protein gives no reaction with other lectins.

[Affinity of pregnant rat-specific beta 1-globulin for different lectins]. / Izuchenie affiniteta spetsificheskogo dlia beremennykh krys beta 1-globulina k razlichnym lektinam.

The pregnancy-specific beta 1-globulin (SBG) reacts with 10 out of 11 lectins which have affinity to monosaccharides (glucose, mannose, galactose and fucose) and acetylamino sugars. The affinity to ConA and PHA-P was the most pronounced while this protein did not react with the pea lectin. The SBG reactions are specific for every lectin (even with the identical carbohydrate specificity). Peculiarities of the SBG reactions with lectins made it possible to reveal a few forms of this protein which differ in the carbohydrate composition and conformation of carbohydrate radicals.

[Effect of trophoblast-specific beta 1-glycoprotein on the ratio of cellular forms in a mast cell population]. / Vliianie trofoblast-spetsificheskogo beta 1-glikoproteina na sootnoshenie kletochnykh form v populiatsii tuchnykh kletok.

The influence of trophoblast-specific beta 1-glycoprotein (TSG) on the degranulation of mast cells and their saturation with heparin was studied. Introduction of the TSG into the population of mast cells of the rat peritoneal fluid practically does not change their degranulation, but lowers the degree of their saturation with heparin. An antibiotic alone increases the saturation of the cells with heparin. The serum of an allergic animal markedly stimulates the degranulation and lowers the degree of saturation of the mast cells with heparin. In an experimental model (antibiotic--the serum of the allergic mast cells) the mast cells transform into very clear (heparin-free) cells and the degree of saturation is at minimum. The TSG introduction into this system stabilizes the population of mast cells and markedly increases the degree of their saturation with heparin. Although the degranulation is rather intensive, it is less expressed, than in the experimental model. This suggests the presence of TSG receptors on the mast cells (targets of allergic reactions). The possibility to use TSG preparations in the therapy of allergic diseases is discussed.

[Biosynthesis of pregnancy-specific beta1-globulin in rats in an in vivo system]. / Izuchenie biosinteza beremennost'-spetsificheskogo beta1-globulina u krys v sisteme in vivo.

It has been demonstrated that pregnancy-specific beta1-globulin is synthesized by the rat placenta. Other organs of pregnant animals (liver, kidneys, lungs, heart, spleen) were incapable of synthesizing this antigen. The greatest amount of pregnancy-specific beta1-globulin is observed in the blood of intact animals on the 11th day after the introduction of ground placental tissue.

[Immunochemical analysis of lectin receptors in the structure of trophoblastic beta 1-glycoprotein and pregnancy-associated alpha 2-glycoprotein]. / Immunokhimicheskii analiz "retseptorov" k lektinam v strukture trofoblasticheskogo beta 1-glikoproteina i assotsiirovannogo s beremennost'i al'fa 2-glikoproteina.

Trophoblastic beta-glycoprotein (TBG), pregnancy-associated alpha 2-glycoprotein (AGP) and alpha-fetoprotein (AFP) bind to concanavalin A, phytohemagglutinin P and pea lectin. Lentil lectin interacts with TBG only, whereas peanut lectin and castor bean lectin are characterized by affinity to AGP. Hence, TBG, AGP and AFP contain the following carbohydrate components: alpha-D-mannose, alpha-D-glucose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine. In addition, AGP contains beta-D-galactose.

[Immunochemical study of the heterogeneity of trophoblastic beta 1-glycoprotein]. / Immunokhimicheskoe izuchenie geterogennosti trofoblasticheskogo beta 1-glikoproteina.

It has been found that in mild acid (pH 6.6) and mild-alkaline media (pH 7.7) both pregnancy proteins form complete precipitates. In more alkaline buffer solutions the form of alpha 2-glycoprotein (alpha 2-GP) precipitate is preserved, while trophoblastic beta 1-glycoprotein (TBG) shows three immunochemically identical components with different electrophoretic mobility. The form with beta-globulins mobility predominates, and minor fragments are presented by alpha- and gamma-components. All TBG forms are clearly seen at pH 8.6. In more alkaline medium (pH 10.0) the clarity of the precipitates drastically decreases. It is shown that heparin introduction into the gel of first dimension electrophoresis increases anode electrophoretic mobility of both proteins at polysaccharide concentration of at least 0.1 mg/ml. Large amounts of heparin cause the increase in TBG alpha-component precipitate area and the decrease in the form with beta-globulins mobility. At the same time alpha 2-GP precipitate area and form remain unchanged.

[Competitive inhibition by carbohydrates of reactions between phytohemagglutinin II and plasma glycoproteins]. / Konkurentnoe ingibirovanie uglevodami reaktsii mezhdu fitogemaggliutininom II i glikoproteinami plazmy krovi.

Competitive reactions between free carbohydrates and the carbohydrates of blood plasma glycoproteins for receptors of phytohemagglutinin II were studied by means of modified cross affinity immunoelectrophoresis. These reactions exhibited both specific and unspecific properties. Possible mechanisms of these reactions are discussed as well as their possible use in studies of properties of carbohydrate-containing biopolymers.

[Physico-chemical characteristics of pregnancy-specific protein in the rat]. / Fiziko-khimicheskaia kharakteristika spetsificheskogo belka beremennosti krys.

Molecular weight of PSP, determined by gel-filtration on Sephadex G-200, is 130 000 +/- 4 000 D and, according to the Laemmli method with SDS, 85 000 +/- 2 000 D. The protein was detected in the zone of beta 1-globulins, its relative electrophoretic mobility is 0.45 +/- 0,2. PSP is heterogeneous by electric charge; at electrofocusing this protein was revealed in the following isoelectric points (pI); 5.85, 6.11, and 6.57. PSP was precipitated with ammonium sulfate (20-50% of saturation). Iron, carbohydrates, lipids were not found histochemically in PSP and it did not manifest the esterase and phosphatase activity.

[Interaction of pregnancy proteins with phytohemagglutinin P and concanavalin A (con A)]. / Vzaimodeistvie belkov beremennosti s fitohemaggliutininom P i konkanavalinom A (kon A).

It has been established that trophoblast-specific beta-glycoprotein and pregnancy-associated alpha 2-glycoprotein specifically react with non-fixed PHA and Con A. Affinity to the former protein is significantly higher than to the latter one. alpha-Fetoprotein has a low affinity to Con A alone. Affinity to this lectin is in an agreement with the content of carbohydrates contained by pregnancy proteins. A considerable part of human serum proteins bind with Con A; receptors for PHA possess only some serum proteins. As the above-mentioned lectins are often used for stimulation of lymphocyte blast transformation, in is recommended that the constituent parts of the culture medium should be preliminarily tested to specify more accurately their affinity to PHA and Con A.

[Immunochemical determination of placenta-specific and interorganic antigens in placental extract and blood serum in pregnant rats]. / Immunokhimicheskoe opredelenie platsentospetsificheskikh i mezhorgannykh antigenov v ékstrakte platsenty i v syvorotke krovi pri beremennosti u krys.

It has been demonstrated that placenta extract of rats contains up to 14 antigens. Moreover, 11 of them are interorgan proteins of wide and limited specificity, two antigens (alpha 1- and alpha 2-globulins) are attributed to acute-phase proteins typical for pregnancy. beta 1-Globulin is a specific protein of rat placenta. The content of these antigens in blood serum increases with pregnancy and reaches a maximum toward the delivery; 3-4 days after delivery beta 1-globulin disappears completely from maternal blood, whereas the concentration of acute-phase proteins drops to the initial level.

[Immunochemical characteristics of alpha 2-globulin from the rat "pregnancy zone" in ontogeny]. / Immunokhimicheskaia kharakteristika al'fa 2-globulina "zony beremennosti" krys v ontogeneze.

An antigen with electrophoretic mobility of alpha 2-globulins was found in the blood serum of the pregnant rats by means of electrophoresis. It is detected not only in the blood serum and tissue extracts of the pregnant rats, but occurs in low concentrations (1 microgram/ml) in the blood serum of the normal adult animals. The concentration of this protein attains the maximal values by the end of the pregnancy period. Alpha 2-globulin appears to be a protein associated with pregnancy.