[Incidence of congenital orthopaedic defect in the martin district (longitudinal survey).]. / Výskyt vrodených ortopedických chýb v okrese Martin (longitudinálne sledovanie).

The authors submit a model of the detection rate, monitoring and treatment of inborn defects of the locomotor system used in the Martin district. During the investigation period from 1972 - 1994 they examined and processed data from 41 281 neonates, i. e. 99,2 % of the total number of liveborn infants in the Martin district, focused specially on the hip joint and inborn defects of the foot. As to clinical symptoms of dysplasia coxae congenita they ascribe the greatest diagnostic value to Ortolani's phenomenon and abduction restricted to less than 60 degrees, which was recorded in 82 % and 52 % of the examined infants resp. As revealed by the incidence of dysplasia and dislocation in different periods, the introduction of preventive and therapeutic measures in the early neonatal stage had an unequivocal positive effect on the incidence of dysplasia and dislocation. The incidence of inborn defects of the foot was on a constant level during the investigation period. The authors did not record a significant coincidence of inborn defects of the foot and dysplasia of the hip joint in the investigated group, which is consistent with data in the literature. In the conclusion the authors emphasize the importance of prevention in the early neonatal age which leads to a reduction of the number of severe secondary coxarthroses. Key words: dysplasia coxae congenita, luxatio coxae congenita, inborn defects of the foot, prevention.

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.

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.

Differences in toxicity and antigenicity between mistletoe lectin I and viscotoxin A 3.

In contrast to mistletoe lectin I (ML I), viscotoxin A 3 does not inhibit protein synthesis in cell-free systems. From the immunological studies it is concluded that ML I and viscotoxin do not share identical structural domains.

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.

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.

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".

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.

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.

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.

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.

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.

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.

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.

[Use of ferritin conjugates of a lectin from mistletoe (Viscum album L.) for the electron microscopic localization of cell surface receptors]. / Die Verwendung von Ferritinkonjugaten eines Lektins der Mistel (Viscum album L.) zur elektronenmikroskopischen Lokalisation von Zelloberflächenrezeptoren.

Ferritin conjugates of a lectin from mistletoe (Viscum album L.) were used for the electron-microscopic demonstration of carbohydrate receptors on the cell surface of human erythrocytes and murine tumor cells. Human A1 erythrocytes showed only a slight focal binding of ferritin. Cells of the mouse ascites tumor strain L 1210 were labelled very tightly on their surface and incorporate the ferritin by pinocytosis. Furthermore they showed cytotoxic changes in their ultrastructure. In the presence of galactose the labelling on the surface, the incorporation of the conjugate within the cell as well as the cytotoxicity were inhibited.