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The N-linked carbohydrate chains of the beta subunit of human chorionic gonadotropin (hCG-beta) isolated from the culture fluid of the choriocarcinoma cell line BeWo were released enzymatically by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F. Subsequently, the O-linked
The glycoprotein hormone hCG and its free alpha-subunit are secreted by the clonal choriocarcinoma cell line JEG-3. Free hCG alpha has a larger apparent mol wt (22,000-24,000) than the combined hCG alpha (18,000-19,000) obtained by dissociation of the hCG secreted by these cells. Techniques
Human chorionic gonadotropin (hCG), purified from the urine of 14 individuals with normal pregnancy, diabetic pregnancy, hydatidiform mole, or choriocarcinoma, plus two hCG standard preparations, was examined for concurrent peptide-sequence and asparagine (N)- and serine (O)-linked carbohydrate
The effects of lectins with different carbohydrate-binding specificities on human hepatoma (H3B), human choriocarcinoma (JAr), mouse melanoma (B16) and rat osteosarcoma (ROS) cell lines were investigated. Cell viability was estimated by uptake of crystal violet. Wheat germ lectin was the lectin with
Crude gonadotropins extracted from the urine of patients with chorioepithelioma (choriocarcinoma) by Bradbury method was purified by a combination of Sephadex gel filtration, CM-C and DEAE-C chromatography. Two biologically active fractions (fraction t-hCG-A and fraction t-hCG-C) were obtained. The
Cell surface carbohydrate chains of human germ cell tumors were investigated histochemically using peanut agglutinin (PNA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin I (UEA-1), and anti-I-(Ma) antibody. Of 16 cases of embryonal carcinoma in adult testis, peanut agglutinin, a
Although amino acid sequences of the alpha- and beta-subunits of human choriogonadotropin (hCG) are known, only limited information is available on the disease state hCG. We have examined the amino acid sequences of the alpha- and beta-subunits of hCG from choriocarcinoma BeWo cells. The amino acid
Human chorionic gonadotropin (hCG) exhibits molecular heterogeneity in both its protein and carbohydrate moieties. This communication describes changes in hCG isoforms detected directly in clinical samples. These isoforms, quantified in blood or urine specimens, show a progression of change
The cultured human choriocarcinoma cell line, JEG-clone 3, secretes substantial quantities of both biologically active hCG and an immunoreactive alpha-subunit (JEG-alpha). This study is concerned with a comparative characterization, using RIA, of the chromatographic properties (via gel exclusion and
Immobilized antibodies are commonly used to recognize and bind proteins of interest from heterogeneous samples; however, subsequent probing of the glycan(s) of captured glycoproteins with lectins is limited by interference due to the competing oligosaccharides inherently present on antibodies. To
A light microscopic analysis of lectin receptors in normal placenta and trophoblastic disease was performed utilizing biotinylated Concanavalin-A (Con-A), wheat germ agglutinin (WGA), and peanut agglutinin (PNA), in conjunction with an avidin-biotin peroxidase complex. Hydatidiform mole, invasive
Human chorionic gonadotropin (hCG) is a specific tumor marker glycoprotein hormone for trophoblastic diseases. It contains 4 asparagine-linked and 4 serine-linked carbohydrate units. Recently, variations in the carbohydrate moieties of hCG in chorio-carcinoma have been suggested. However, the
Human chorionic gonadotropin (hCG) highly purified from the urine of patients with trophoblastic diseases (choriocarcinoma and hydatidiform mole) and from healthy pregnant women contains four asparagine-linked sugar chains in one molecule. Comparative studies of the sugar chains released by
A panel of monoclonal antibodies directed at fucosylated and sialylated carbohydrates on the Type 1 and Type 2 blood group precursor chains was used in an immunohistological study of trophoblast subpopulations. Formalin-fixed paraffin-embedded sections of normal trophoblast throughout pregnancy,