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Biomedical subjects

U Pfüller

Publications and source records attributed to U Pfüller.

10 recordsLinked to original sources

Carbohydrate specificity of the receptor sites of mistletoe toxic lectin-I.

The carbohydrate specificity of mistletoe toxic lectin-I (ML-I) was studied by haemagglutination-inhibition assay. The results indicated that ML-I has a broad range of affinity for Gal alpha,beta linked sequences. The galabiose (E, Gal alpha 1----4Gal) sequence, a receptor of the uropathogenic E. coli ligand, was one of the best disaccharide inhibitors tested. The lectin also exhibits affinity for Lac(Gal beta 1----4Glc), T(Gal beta 1----3GalNAc), I/II(Gal beta 1----3/4GlcNAc) and B(Gal alpha 1----3Gal) sequences. Gal alpha 1----4Gal and Gal beta 1----4Glc are frequently occurring sequences of many glycosphingolipids located at the mammalian cell membranes, such as intestinal and red blood cell membranes, for ligand binding and toxin attachment. This finding provides important information concerning the possible mechanism of intoxication of cells by the mistletoe preparation.

Binding Sites

[Electronmicroscopic-histochemical demonstration of acid mucopolysaccharides using cationic ferrocenyl compounds (author's transl)].

Long-chain ammonium compounds with ferrocenyl groups were synthesized and used for the light (sudanophilia) and electron microscopic (electron dense staining by the iron of the ferrocenyl group) localisation of acid mucopolysaccharides. At least 5 of the 39 prepared ammonium salts produce a very good contrast. Cetyl-ferrocenylmethyl-dimethyl ammonium chloride has been found to be the best blocking agent and stain for acid polysaccharides.

Animals

Sudan Black B: chemical structure and histochemistry of the blue main components.

Sudan Black B contains two blue main components, SSB-I and SSB-II. Their chemical structures were determinated by the aid of two-dimensional thin-layer chromatography, column chromatography, absorption, IR, mass, H1-NMR, and C13-NMR spectroscopy and were proved by alternate synthesis. SSB-I has been found to be 2,3-dihydro-2,2-dimethyl4-[(4-phenylazo-1-naphthalenyl)-azol]-1H-perimidine. For SSB-II was confirmed the known structure 2,3-dihydro-2,2-dimethyl-6-[(4-phenylazo-1-naphthalenyl)-azo]-1H-permidine. Relations of chemical structure of SSB-I and SSB-II to their staining properties are discussed.

Azo Compounds

[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

[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