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1.
Vnitr Lek ; 36(12): 1172-6, 1990 Dec.
Article in Czech | MEDLINE | ID: mdl-2284714

ABSTRACT

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.


Subject(s)
Hepatitis B Surface Antigens/analysis , Hepatitis B/prevention & control , Organ Transplantation/adverse effects , Tissue Donors , Enzyme-Linked Immunosorbent Assay , Hepatitis B/etiology , Humans
3.
Cas Lek Cesk ; 128(25): 777-80, 1989 Jun 16.
Article in Czech | MEDLINE | ID: mdl-2527600

ABSTRACT

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.


Subject(s)
Hepatitis B Antibodies/analysis , Viral Hepatitis Vaccines/analysis , Hepatitis Antibodies/analysis , Hepatitis B Surface Antigens/immunology , Hepatitis B Vaccines , Hepatitis Delta Virus/immunology , Immunoglobulin G/analysis , Immunoglobulin G/immunology
5.
Biomed Biochim Acta ; 46(2-3): S192-6, 1987.
Article in English | MEDLINE | ID: mdl-3593297

ABSTRACT

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.


Subject(s)
Anemia, Hemolytic/blood , Erythrocyte Membrane/metabolism , Pyruvate Kinase/deficiency , Reticulocytes/metabolism , Humans , In Vitro Techniques , Membrane Proteins/blood , Molybdenum/blood , Pyruvate Kinase/blood , Spectrin/metabolism
6.
Comp Biochem Physiol B ; 86(3): 531-5, 1987.
Article in English | MEDLINE | ID: mdl-3595088

ABSTRACT

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.


Subject(s)
Ascorbic Acid/metabolism , Blood Proteins/metabolism , Membrane Proteins/metabolism , Molybdenum/metabolism , Spectrin/metabolism , Animals , Brain/metabolism , Cattle , Erythrocyte Membrane/metabolism , Humans , Intestine, Small/metabolism , Mice , Microvilli/metabolism , Protein Binding , Rabbits , Rats , Species Specificity , Structure-Activity Relationship , Synaptic Membranes/metabolism
18.
Cell Biochem Funct ; 2(1): 21-2, 1984 Jan.
Article in English | MEDLINE | ID: mdl-6467511

ABSTRACT

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.


Subject(s)
Molybdenum/metabolism , Spectrin/metabolism , Binding Sites , Erythrocyte Membrane/metabolism , Humans , In Vitro Techniques , Protein Conformation
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