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Biomedical subjects

M Kselíková

Publications and source records attributed to M Kselíková.

At least 19 recordsLinked to original sources

[Prevention of viral hepatitis B transmission in the transplantation program].

The authors discuss possible detection of HBsAg with regards to demands of the transplantation programme. They compared the sensitivity of HBsAg detection by ELISA on kits of various firms, using a panel of sera previously examined by the RIA technique. The most sensitive and most rapid answer on the presence of a surface antigen of the hepatitis B virus by the ELISA technique can be obtained using a Wellozyme kit of Wellcome Diagnostics Co., i.e. within 60 minutes. The firm must, however, equip the kits with double volumes of positive and negative controls.

Enzyme-Linked Immunosorbent Assay↗

[Detection of antibodies and assessment of an international unit of anti-HBs specific immunoglobulin, HEPAGA].

The authors submit information on the presence and titre of antibodies against antigens of the hepatitis B virus [HB] and the Czechoslovak specific anti-HBs immunoglobulin, HEPAGA, and on the presence of the delta-antibody. The presence of the antibody against the surface antigen of the HB virus [HBsAb, anti-HBs] was examined in 32 batches, the antibody against the nucleus of the HB virus [HBcAb] and e-antigen [HBeAb] in a total of 27 batches. HBsAb was positive in the majority of cases still when diluted 1/2,500,000; HBcAb when diluted in the range from 1/25,000 to 1/2,500,000; the positivity of HBcAb ended with the exception of one batch at the dilution of 1/250. The delta antibody was detected only in batches from 1982 and 1983, in a maximum dilution of 1/8. All examinations were made by the radioimmunoassay [RIA] technique. The authors give also an account of the assessment of the international HEPAGA [IU/ml]. The last batch has 170 IU/ml.

Hepatitis Antibodies↗

Structural analogy among mammalian spectrins and spectrin-like proteins revealed by molybdenum labeling.

Pentavalent complex of 99Mo with ascorbic acid binds in vitro to the plasma membranes of human, rabbit, rat and mouse red cell membranes and to bovine synaptic and rat intestinal brush border membranes. Red cell spectrins and spectrin-like proteins from non-erythroid cells were determined as the molybdenum-binding proteins in the membranes. Specificity of this binding among all membrane proteins suggests structural analogy in this group of proteins.

Animals↗

Reticulocyte-dependent labeling alterations of red cell membrane in pyruvate kinase deficiency anemia.

The radioactive labeling of spectrin using the pentavalent complex of molybdenum-99 was applied to the study of membrane protein in pyruvate kinase deficient red cells. Compared to the control, the labeling profile of the enzymopathic red cell membrane proteins remained generally unchanged but the molybdenum uptake was found to depend largely on the reticulocyte count. This finding may reflect changes during the cell maturation.

Anemia, Hemolytic↗

Specific molybdenum binding to spectrin subunits.

Molybdenum in the form of its pentavalent complex binds primarily to spectrin when incubated with erythrocytes. Only the band 1 subunit is involved in this interaction thus indicating some structural differences between spectrin subunits.

Binding Sites↗

Unchanged binding of 99molybdenum to red cell membrane proteins in hereditary spherocytosis.

The interaction of 99Mo with red cell membrane proteins was found specific for spectrin both in normal red cells and those of hereditary spherocytosis. In addition, no significant quantitative differences were observed in labeling patterns between these two types of red cells, thus indicating no major alterations in the spectrin molecules of hereditary spherocytosis.

Blood Proteins↗