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vicia unijuga/carbohydrate
Veza se sprema u međuspremnik
8 rezultati
Purification and characterization of anti-N lectin from Vicia unijuga leaves.
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1. An anti-N lectin was extracted from Vicia unijuga leaves with phosphate-buffered saline (PBS). Purification of the lectin was achieved, after pretreatment of the PBS extract by ammonium sulfate fractionation and absorption with human M erythrocytes, by using a combination of conventional
Biosynthesis of Vicia graminea lectin- and Vicia unijuga lectin-binding glycoproteins in human tumor and nontumor cells and an estimation of its epitope structure.
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We investigated biosynthesis of Vicia graminea lectin (VGA)- and Vicia unijuga lectin (VUA)-binding (Vgu) glycoproteins, which are human malignant tumor-associated antigens, in cultured human tumor and non-tumor cells by pulse-labeling experiments with [35S]-methionine, followed by
Isolation and characterization of a Vicia graminea and Vicia unijuga lectins-binding (Vgu) glycoprotein with Thomsen-Friedenreich (T) activity from human liver metastases of pancreas carcinoma.
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1. Perchloric acid-soluble fraction from liver metastases of pancreas carcinoma of a patient with blood group B, was subjected to a systematic affinity chromatography using Vicia unijuga lectin (VUA) and Arachis hypogaea anti-T lectin (PNA) as immobilized ligands and separated into three fractions,
Presence of Vicia graminea lectin- and Vicia unijuga lectin-binding (Vgu) glycoprotein in human amniotic fluid and some of its chemical and serological properties.
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Vicia graminea- and Vicia unijuga-binding glycoprotein (Vgu glycoprotein) has been reported as a malignant tumor-associated antigen, which is found in various kinds of malignant tumor-tissues and ascitic and cyst fluids of malignant tumor patients, but not found in 20 kinds of normal human tissues.
[Serological property of perchloric acid-soluble glycoprotein fractions of human meconium].
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Perchloric acid-soluble fractions (PASFs) were separated, in yields of 87.0-151.9 mg per 1.0 g of wet meconium sample, from six samples of human meconium, and identified as glycoproteins having 41.2-74.1% carbohydrate by chemical composition analysis. Six PASFs reacted with anti-A, -B, -Lea and -Leb
Isolation and characterization of blood group N antigen precursor glycoproteins with Thomsen-Friedenreich (T) activity, N antigen precursor glycoproteins and T-active glycoproteins from cyst fluids of malignant ovarian clear cell carcinoma.
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1. Two perchloric acid-soluble glycoprotein fractions from cyst fluids of 2 patients with ovarian clear cell carcinoma in malignant were subjected to a systematic affinity chromatography using Vicia unijuga lectin-Cellulofine column and Arachis hypogaea lectin-Cellulofine column and separated into
Separation and biochemical characterization of blood group N antigen precursor glycoproteins with Thomsen-Friedenreich (T) activity, T-active glycoproteins and N antigen precursor glycoproteins from ascites of primary ovarian cancer patients.
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1. Three perchloric acid-soluble fractions from ascites of three primary ovarian cancer patients were subjected to Sephacryl S-300 gel filtration, respectively, and three Fr. 1 which were eluted in the vicinity of void volume as minor fractions, were then separated by a systematic affinity
Biochemical characterization of glycoprotein components in human ovarian cyst fluids by lectins.
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1. Perchloric acid-soluble glycoprotein fractions (PASFs) were separated, in yields of 180-610 mg per 100 ml of cyst fluid, from the cyst fluids of human ovarian cystadenomas (OCAs) in benign and borderline and ovarian clear cell carcinoma (OCC) in malignant, and then identified as glycoproteins
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