vicia unijuga/lectin

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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

[Vicia graminea lectin or Vicia unijuga lectin-binding (Vgu) glycoproteins as new tumor-associated substances].

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The purification and serological and chemical properties of Vicia graminea lectin (VGA) and Vicia unijuga lectin (VUA) were described, and then the binding-specificity of anti-M and -N antibodies and both the lectins was discussed in this review. On the basis of the facts that Vgu glycoproteins

Presence of Vicia graminea lectin- and Vicia unijuga lectin-binding (Vgu) glycoproteins in human fetal membranes and some of their biochemical properties.

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We have previously reported that Vicia graminea lectin (VGA)- and Vicia unijuga lectin (VUA)-binding glycoproteins (Vgu glycoproteins), malignant tumor-associated antigens, exist in human meconium and amniotic fluid. To examine the origin of Vgu glycoprotein, their presence, some of their chemical

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

Presence of Vicia graminea lectin- or Vicia unijuga lectin-binding (Vgu) glycoproteins, Vgu glycoproteins with Thomsen-Friedenreich (T) activity and T-active glycoproteins in human meconium.

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Perchloric acid-soluble fraction prepared from a mixture of meconiums of 22 newborn babies was subjected to a systematic affinity chromatography using Vicia unijuga lectin-Cellulofine column and Arachis hypogaea lectin-Agarose column and separated into four fractions, Vgu glycoprotein, Vgu

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 or Vicia unijuga lectin-binding (Vgu) glycoproteins with and without Thomsen-Friedenreich (T) antigen in normal human seminal plasma.

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Vgu glycoprotein (Vicia graminea lectin- or Vicia unijuga lectin-binding glycoprotein) has been reported as oncofetal antigen, which is found in many kind of tumor tissues, amniotic fluid and fetal membranes. In autoradiography with an 125I-labeled Vicia unijuga lectin (VUA) probe and an

Investigation of Vicia graminea lectin- and Vicia unijuga lectin-binding glycoproteins as novel oncofetal antigens in cyst and ascitic fluids of human ovarian tumors in benign, dysplastic, and malignant stages.

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Perchloric acid-soluble fractions (PASFs) were obtained from cyst fluids of human benign ovarian mucinous cystadenoma, benign dermoid cyst, "borderline" mucinous cystadenoma, and malignant ovarian clear cell carcinoma, and from fluids of malignant embryonal carcinoma and malignant serous

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.

Presence of a Vicia unijuga lectin-binding (Vgu) glycoprotein with Thomsen-Friedenreich (T) activity and Vgu glycoproteins in human primary hepatocellular carcinoma.

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1. Twenty perchloric acid-soluble glycoprotein fractions (PASFs) were separated from carcinomatous and non-carcinomatous regions of the livers of 5 patients with primary hepatocellular carcinoma (HCC) and 5 patients with a complication of HCC and hepatocirrhosis (HC). 2. In autoradiography using

A new source of anti-N lectin: leaves of the Korean Vicia unijuga.

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[Highly specific anti-N lectin from the leaves of Vicia unijuga A. Br].

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Vicia graminea lectin- or Vicia unijuga lectin-binding (Vgu) glycoproteins as new oncofetal antigens.

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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

[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

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