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Biomedical subjects

P Ziska

Publications and source records attributed to P Ziska.

At least 19 recordsLinked to original sources
PubMed1989

Detection and quantification of ligand leakage from lectin affinity columns.

The usefulness of lectin affinity chromatography for the preparation of glycoproteins is impaired by ligand release. Ligand leakage from mistletoe lectin (MLI) Sepharose 4B column was detected by 24 h skin reaction in mice and by immunoblotting. Immunoaffinity chromatography was found to be an efficient method for the separation of lectin traces from the glycoprotein fraction. A sugar concentration dependent increase of lectin release from MLI-Sepharose 4B column was detected by a solid phase enzyme immunoassay.

Animals↗
PubMed1984

Immunological reactivity of tumor associated glycoproteins prepared by affinity chromatography.

Crude 3M KCl extracts prepared from tumor tissue and ascitic tumor cells of methylnitrosourea-induced fibrosarcoma of CBA mice or of a human stomach adenocarcinoma were gelfiltrated on Ultrogel AcA 34. Single fractions of these preparations were incubated with spleen cells of tumor bearing mice or blood peripheral lymphocytes. The response was detected by MEM-technique. Antigenic activities were found in molecular weight ranges from 200 to 300 kD (P1) and from 40 to 70 kD (P2). Single glycoproteins of the P1- and P2-fractions could be separated by affinity chromatography on immobilized D-galactose specific mistletoe lectin I, as detected by electrophoresis on microgradient gels (1.2-40%) or on SDS polyacrylamide slab gels. Especially the isolated glycoproteins of the P1-fractions are responsible for the observed antigenic reactivity, assayed in vitro by the MEM-technique and in vivo by foot pad swelling test.

Adenocarcinoma↗
PubMed1982

Isolation and characterization of a lectin from garden cress (Lepidium sativuum).

A lectin has been isolated from extracts of garden cress (Lepidium sativum) by affinity chromatography on human immunoglobulin-Sepharose. The lectin reacts with human erythrocytes without specificity for the A, B and 0 blood group. Erythrocytes of animal origin are also agglutinated by the lectin. The hemagglutinating activity is abolished by heating the lectin solution at 70 degrees C or by dialysis against strong acid buffers. The hemagglutination reaction is not inhibited by monosaccharides. Lectin-glycoprotein interactions are described and discussed.

ABO Blood-Group System↗
PubMed1982

The toxic A-chain of mistletoe lectin I: isolation and its effect on cell-free protein synthesis.

The reduction of Sepharose bound mistletoe lectin I (ML I) is a convenient method for preparing A- and B-chains under mild conditions. The B-chain represents the D-galactose binding moiety. The A-chain shows a significant dose-dependent inhibition of protein synthesis in cell-free systems from rat liver and rabbit reticulocytes, while pure B-chain preparations do not affect ribosomal translation processes.

Animals↗
PubMed1981

Isolation and properties of three lectins from mistletoe (Viscum album L.).

Three lectins have been isolated from an extract of mistletoe (Viscum album) by affinity chromatography on partially hydrolysed Sepharose and human immunoglobulin- Sepharose. The lectins differ in molecular weight and sugar specificity (lectin I, mol.wt. 11500, D-galactose-specific; lectin II, mol.wt. 60000, both D-galactose- and N-acetyl-D-galactosamine-specific; lectin III, mol. wt. 50000, N-acetyl-D-galactosamine-specific). All three lectins react with human erythrocytes without specificity for the A, B, and O blood groups. In contrast with abrin and ricin the mistletoe lectins cannot be divided into "toxins" and "haemagglutinins".

Carbohydrates↗
PubMed1980

The lectins from Agaricus edulis. Isolation and characterization.

2 lectins from the mushroom Agaricus edulis were isolated, after heating the crude extract at 75 degrees C, by ion exchange chromatography and gel chromatography using QAE-Sephadex A-50 and Sephadex G75. Some hemagglutinating and physicochemical properties of the agglutinins are reported.

Agaricales↗
PubMed1980

Inhibition of protein synthesis by a toxic lectin from Viscum album L. (mistletoe).

1. The haemagglutinating and toxic lectin from Viscum album L. (mistletoe) inhibits protein synthesis in a lysate of rabbit reticulocytes, with an ID50 (concentration giving 50% inhibition) of 2.6 microgram/ml. This effect is enhanced (ID50 0.21 microgram/ml) if the lectin is reduced with 2-mercaptoethanol. 2. The lectin inhibits protein synthesis also in BL8L cells in culture. Inhibition occurs after a lag time of 3 h. The ID50 is 7 ng/ml, and increases after reduction of the lectin. 3. This and the gross lesions observed in rats poisoned with V. album lectin indicate this is a toxin very similar to ricin.

Animals↗
PubMed1980

Electron microscopic visualization by the unlabelled lectin/antiferritin-antibody/ferritin method of lectin receptors on cell surfaces.

For electron microscopic demonstration of carbohydrate moieties on cell surfaces of HeLa-cells the lectins from Viscum albumin, Canavalia ensiformis and Dolichos biflorus have been used. The staining experiments were performed by reaction of the cell surface receptor localized lectin with purified antiferritin-antibody followed by ferritin. The three-step reaction cell surface receptors leads to lectin leads to antiferritin antibody leads to ferritin is proposed as general method for electron microscopic localization of lectin receptors without covalent coupling.

Antibodies↗
PubMed1979

Combination of immunological and lectin reactions in affinity histochemistry: proposition of the term affinitin.

Using the series system cell receptor leads to mistletoe lectin leads to antiferritin-antibody leads to ferritin, the possibilities for combination of lectin and immunological reactions for histochemistry are discussed. The system cell antigen leads to antibody leads to labelled mistletoe (or other) lectin is recommended for visualization of cell antigens (mistletoe lectin as common immunoglobulin reagent). It is pointed out that lectin reactions do not belong to immunhistochemistry but to affinity histochemistry. For all receptor specific proteins (antibodies, lectins, enzymes, haptoglobin and other) the term affinitin is proposed. In consideration of this new definition a common scheme is formulated: Affinitin reacts with affinitin receptor forming affinity product.

Animals↗
PubMed1979

Affinity chromatography of human serum proteins using matrix bound lectin from Viscum album L.

The D-galactose specific lectin from Viscum album L. reacts with serum proteins that contain the corresponding D-galactopyranosyl residues. By affinity chromatography of human serum on lectin-sepharose IgM, alpha 2-macroglobulin, haptoglobin and beta-lipoprotein were quantitatively retained. Only parts of IgA, IgG and transferrin were retarded. The other serum proteins are unbounded as albumin, beta 1 A- and beta 1 C-globulin.

Chromatography, Affinity↗
PubMed1979

Affinity chromatography of human serum proteins using matrix bound lectins from Viscum album and Vicia faba.

The D-galactose specific lectin from Viscum album and the D-mannose specific lectin from Vicia faba react with serum proteins which contain the corresponding carboyhydrate moieties. By affinity chromatography of human serum using the combination of insolubilized lectins coupled to Sepharose it is possible to fractionate serum proteins in 3 groups: 1. proteins which react with both of the lectins; 2. proteins which react only with one of the lectins; 3. proteins which do not display any affinity for one of the two lectins.

Blood Proteins↗
PubMed1979

Chemical modification studies on the D-galactopyranosyl binding lectin from the mistletoe Viscum album L.

The role of amino, sulfhydryl, disulfide, carboxyl, phenolic, imidazole and indole groups on the agglutination of human erythrocytes by the lectin from Viscum album has been determined using specific chemical modification techniques. The results indicate that tyrosine residues participate in the hemagglutination reaction. Subunits of the lectin possess only reduced hemagglutinating ability.

Borohydrides↗