vicia graminea/lectin

Crude extracts of Vicia graminea seeds agglutinate human N erythrocytes as anti-N immunsera. The anti-N lectin is purified after precipitations with ammonium sulphate of crude extracts, DE52 Whatman chromatography and sephadex G150 gel filtration. Its homogeneity is demonstrated by physical and

The subunit of the Vicia graminea lectin with blood-group-N specificity was examined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and gel filtration in 6M-guanidinium chloride, and its molecular weights was found to be 25 000. The unique N-terminal sequence fof the first nine

Vicia graminea lectin, purified by affinity chromatography, was homogeneous in sodium dodecylsulphate/polyacrylamide gel electrophoresis and migrated with a velocity corresponding to a molecular weight of 125 000. Heating of 0.1% sodium dodecylsulphate at 100 degrees C caused dissociation of the

Purified Vicia graminea lectin, isolated from seeds, was found to contain D-mannose, 2-acetamido-2-deoxy-D-glucose, L-fucose, D-galactose, and D-xylose in the molar ratios approximately 3.9:1.5:1.2:1.1:1.0. The oligosaccharides, obtained after hydrazinolysis of Vg-lectin, were N-reacetylated,

A lectin with N blood group specificity was isolated from Vicia graminea seeds. This lectin was purified from a crude extract by precipitation with ammonium sulfate, DEAE-cellulose chromatography and Sephadex G-150 gel filtration. Purification steps were followed by increase of specific activity.

The erythrocyte receptors for Vicia graminea (Vg) anti-N lectin have been investigated after 125I-labelling of the purified lectin and binding to membrane components separated by dodecyl sulphate polyacrylamide gel electrophoresis. GP alpha (synonym glycophorin A or MN glycoprotein) and GP delta

Binding of the radioactive Vicia graminea lectin to human blood-group M and N erythrocytes and to horse erythrocytes was studied at pH 6-10. Binding of the lectin to untreated human erythrocytes and to those treated with Vibrio cholerae neuraminidase increased severalfold from pH 6 to pH 8 and was

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

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

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

A sample of polyagglutinable red cells was obtained from a healthy individual (group O, N) possessing a hemoglobin (Hb) variant called Hb M-Hyde Park. The sialic acid content of the individual's red cells is 90 percent of normal, and his cells are agglutinated by monoclonal but not lectin anti-Tn, a

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,

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

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

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.