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Biomedical subjects

H Franz

Publications and source records attributed to H Franz.

At least 109 records · Page 6Linked to original sources
PubMed1977

[Isolation and characterization of mistletoe extracts (Viscum album L.). II. Effect of agglutinating and cytotoxic fractions on mouse ascites tumor cells].

Lectin from mistletoe (Viscum album L.) was studied for its relations with the toxins from Viscum album, ascites tumor cells of mouse, and human immunoglobulins. Using affinity chromatography on glutaraldehyde-crosslinked IgG (human) from viscum crude extract, a fraction was isolated which exhibited full agglutination capacity and high toxicity. The supernatant showed no agglutination capacity but a strong toxic effect on mouse ascites tumor cells. This toxic effect could not be influenced by further additions of insolubilized IgG. Chromatography on DEAE cellulose also gave agglutinating fractions with toxic effects and a non-agglutinating toxic portion. Column chromatography on Sephadex G 75 allowed separation of toxic from agglutinating components. The molecular weight of the toxin remaining after lectin removal was above 10,000. Lectin was found to bind more readily to mouse ascites tumor cells than to erythrocytes.

Animals↗
PubMed1977

[Isolation and characterization of mistletoe extracts (Viscum album L.). I. Affinity chromatography of mistletoe extracts on immobilized plasma proteins].

The agglutinating effect of lectin from mistletoe (Viscum album L.) relative to erythrocytes and tumor cells is destroyed or reduced by plasma proteins. There is a competition between lectin receptors of plasma proteins, especially immunoglobulins and erythrocytes, as well as tumor cells. The preparation of insolubilized immunoglobin fractions allows one to separate lectin from the mistletoe extract. There exist chemical connections between the lectin fixed to the adsorbent and part of the toxic components.

Blood Proteins↗
PubMed1977

[A method for the preparation and purification of the two blue main components of sudan black B (author's transl)].

Two dimensional thin layer chromatography of four commercial samples of Sudan Black B reveals two blue main components (SSB I and II) and at least 38 further fractions. The quantitative composition of one sample was estimated. SSB-I and SSB-II were isolated and purified by column chromatography supplying amounts for histochemical use. Histochemical experiments are described.

Chromatography, Thin Layer↗
PubMed1976

[Effect of protamine sulphate on erythrocyte agglutination by anti-rh antisera. Cause of time-dependence (author's transl)].

The effect of protamine sulphate on Rh antisera causes agglutination also in saline milieu and is time-dependent. Synchronous to the serologically demonstrable decrease of the protamine concentration a normalization of the immunoelectrophoretic picture (especially of the albumin arc) and a decline of the precipitate formation by heparin occur. These effects are based on enzymatic degradation of protamine by a protaminolytic enzyme contained in human serum. This enzyme could not be inhibited by sodium fluoride, sodium azide, ammonium oxalate, EDTA or alpha, alpha'-dipyridyl to a serologically desired degree. The change of the behaviour with regard to agglutination of human erythrocytes in the system Rh antibody - protamine sulphate results primarily from blocking acid groups on the erythrocyte surface and not from chemical modification of IgG antibodies. In this system protamine sulphate leads to the formation of agglutinates but it does not represent an obligate constituent of the formed agglutinate.

ABO Blood-Group System↗
PubMed1975

Ultrastructural detection of lectin receptors by cytochemical affinity reaction using mannan-iron complex.

A two-step affinity reaction is described for electron microscopic demonstration of the Concanavalin A as well as the Lens culinaris lectin receptors by means of the yeast mannan-iron complex. First the tissue was incubated in the lectin. Afterwards the incubation in the yeast mannan-iron complex was performed and reaction takes place between the still free second sugar binding site of membrane bound lectin molecules and the polysaccharides. This membrane receptor-lectin-polysaccharide complex is revealed by the electron dense iron core of the yeast mannan-iron complex. The specificity of the reactions could be demonstrated by addition of the hapten or by incubation in the yeast mannan-iron complex only. The proposed technique has proved useful for demonstration of lectin receptors in the small intestine.

Animals↗