[Implementation of fluorescent imaging technology in endovideosurgical treatment of colorectal endometriosis].

The article includes a clinical case of a patient with deep infiltrating endometriosis with rectum involving and using intraoperative controlled fluorescence in order to increase the radicality of surgery and improve the prognosis of the disease. Surgical excision of the endometrioitic nodules is the only effective way of treating patients with colorectal endometriosis in terms of relieving pain, improving quality of life and restoring reproductive function. The possible types of surgical interventions can be performed: endometrioid lesion shaving, discoid or circular intestinal resection with anastomosis.

Highly Sensitive Immunochromatographic Identification of Tetracycline Antibiotics in Milk.

A rapid immunochromatographic assay was developed for the control of tetracycline (TC). The assay is based on the competition between immobilized TC-protein conjugate and TC in a tested sample for binding with polyclonal anti-TC antibodies conjugated to colloidal gold during the flow of the sample along a membrane strip with immobilized reactants. Conjugation of colloidal gold and the total immunoglobulin (IgG) fraction of polyclonal antibodies was used to increase the assay sensitivity to ensure low content of specific antibodies in the conjugate.

[Interaction of triiodothyronine-biotin conjugate with binding proteins in immunoassay systems].

A new construction of a test-system for free thyroid hormone 3,3',5-triiodothyronine determination (free T3) in human blood serum in ELISA and IRMA variants was described. For this purpose a low-molecular weight bifunctional conjugate containing T3 and vitamin H (biotin, Bt) residues was synthesized. The conjugate (T3-Bt) can be bound via its biotin function to biotin-binding proteins on a solid phase whereas its T3-portion can interact with monoclonal antibody against T3 (anti-T3-MAb) labeled with horseradish peroxidase or iodine-125 in an enzyme immunoassay or an immunoradiometric assay system (ELISA or IRMA), respectively.

[The biotin-thyroxin conjugate as a bifunctional ligand of binding proteins].

The conjugate of the residue of vitamin H (biotin, Bt) with the hormone of thyroid gland thyroxin (T4) was prepared by N-acylation of N-(3-aminopropyl) biotin amide with N-hydroxysuccinimide ester of N-acetyl thyroxin. The interactions of the Bt-T4 conjugate with one or simultaneously with two binding proteins with affinity to Bt or T4 in solution and on a solid phase were studied by electron spectroscopy, enzyme immunoassay, and computer modeling. Bt-T4 was specifically fixed in the Bt-binding site of the streptavidin molecule via a large number of hydrogen bonds and hydrophobic interactions.

[Precipitation of streptavidin complexes with biotinylated proteins in agar gel].

The effect of precipitation of complexes of streptavidin with biotinylated proteins under conditions of simple (according to Mancini) and double (according to Ouchterlony) radial diffusion in agar gel was studied. The position and form of precipitation lines depended primarily on the initial concentration of components and the degree of protein biotinylation. Free biotin, 1% SDS, and 6 M urea contained in the gel, as well as thermal denaturation of streptavidin inhibited the precipitate formation.

[Characteristics of immunoaffinity chromatography and a new method for isolation of human thyroid peroxidase from subcellular fractions of thyroid gland].

A system for quantitative determinations of human thyroid peroxidase (TPO) in biological fluids has been obtained, based on the use of enzyme-linked immunosorbent assay. Immunochemical properties of TPO were studied under variable conditions, and a new method for isolating the protein from microsomes, mitochondria, and cytosol of thyroid glands of patients with diverse thyroid diseases was developed. The procedure involves solubilization of subcellular fractions with detergents, their sonication, two sequential runs of chromatography (on sorbents with immolbilized monoclonal antibodies against TPO and goat anti-human immunoglobulin antibodies), treatment with ribonuclease, and dialysis.

[Characteristics of monoclonal antibodies against human thyroid peroxidase for use in immunoaffinity chromatography and immunoassays].

Two types of monoclonal antibodies (MABs) against human thyroid peroxidase (TPO) have been obtained, which interact with spatially separated conformational epitopes of the antigen (Ka values are in the range 10(8)-10(9) M(-1)). The binding site of MAB F8 is in the immunodominant region of the TPO molecule, in the vicinity of the autoantigenic determinants, whereas the epitope specific for MAB A1 lies outside this location. Both MABs retain the ability to form immune complexes after solid-phase immobilization and chemical modification with a biotin derivative.

[Autoantibodies to human thyroid peroxidase in immunoassay and immunoaffinity chromatography].

A biochemical system of radioimmunoassay of human thyroid peroxidase (TPO) with the use of specific autoantibodies was developed for the first time. This system includes lyophilized preparations of human autoantibodies to TPO, radioiodinated TPO, standards prepared from pure TPO, and the solid-phase protein A as a precipitating agent. An analytical system was used to study the TPO distribution in fractions of thyroid tissue homogenate.

[Interaction of transcortin with human syncytiotrophoblast].

Interactions of transcortin (corticosteroid-binding globulin, CBG) variants, nCBG and rCBG, present in the blood of pregnant women, and microvesicular fraction of the brush border membrane of human placental syncytiotrophoblast at 23 +/- 2 degrees C were studied. Interaction of nCBG in complex with a steroid with each of the two types for specific binding was found associated with transmembranous transfer of glycoprotein. Interaction of rCBG with binding sites of both types did not involve subsequent glycoprotein transfer through the membrane.

[The effect of steroids on binding of transcortin with human syncytiotrophoblasts].

The effects of steroids on specific binding of transcortin (corticosteroid-binding globulin, CBG) variants (nCBG and vCBG) from pregnant women sera to the microvesicular membrane fraction derived from placental syncytiotrophoblast brush border have been studied. It was shown that native CBG variants stripped of steroids lose their ability to interact with specific membrane sites. Specific binding of CBG variants was found to increase in parallel with an increasing per cent content of glycoproteins associated with cortisol, reaching a maximum at cortisol concentrations of 5.

Transcortin does not restrict the transmembrane transfer of cortisol.

We have studied the specific binding of both free and transcortin-bound cortisol to the microvesicles derived from the brush border of the plasma membrane of human placental syncytiotrophoblast. Kinetics of the steroid binding to these microvesicles was found to be independent on cortisol being complexed with transcortin. Both cortisol and transcortin were accumulated in the inner space of the microvesicles.

[Variety of transcortin in the blood of women during normal pregnancy].

A concentration of pregnancy-related transcortin variety was detected in the venous blood serum of women at varying time of normal pregnancy and after delivery as well as in umbilical and retroplacental blood serum using a radio-immunoassay. This transcortin variety was found in the blood at early stages of pregnancy (the end of the 1st-the start of the 2nd trimester). During pregnancy the content of this variety increased, mainly in the 2nd trimester.

[Pregnancy-associated variant of transcortin in humans].

Properties of the human transcortin variety related to pregnancy were studied. The transcortin variety has been found in retroplacental blood serum and differed from the glycoprotein of healthy donors by the structure of carbohydrate moiety. Physico-chemical and immunochemical properties of the transcortin variety studied, specific mainly to its polypeptide component, were similar to the properties of transcortin from blood of healthy donors.

[Comparative study of human transcortin isolated from normal donor blood and retroplacental blood].

It was demonstrated that the physico-chemical properties of human transcortin, i.e., electrophoretic, hydrodynamic and immunochemical characteristics, amino acid composition, steroid binding parameters, do not depend on the source of the glycoprotein (male or female blood, retroplacental blood).

[Characterization of human retroplacental blood plasma proteins isolated by biospecific chromatography on immobilized cortisol].

Human retroplacental blood plasma proteins with affinity for cortisol were isolated by biospecific chromatography and identified by electrophoretic and immunochemical methods as alpha1- and beta1-globulins and IgG. IgM and IgA immunoglobulins. A high specific affinity for cortisol (Kas = 1,5 .