Biomedical subjects

L Grubhoffer

Publications and source records attributed to L Grubhoffer.

40 records · Page 3Linked to original sources

PubMed1987

Peroxidase labelled mumps virus antigens and their application in IgM capture immunoassay: first experience.

Three types of mumps virus antigen have been prepared: virion antigen (MV); soluble nucleoprotein (NP) antigen; envelope glycoprotein (eGp) antigen. These antigens were coupled directly with horse-raddish peroxidase and tested by IgM-capture technique against selected human sera. The advantage of the suggested design, in addition to general superiority of the IgM-capture systems, lies in its selectivity achieved by introducing a monoclonal antibody for IgM binding and in time saving due to the use of labelled antigen without the loss of sensitivity and specificity. The assay fulfils the criteria for quick viral diagnostic. Our first experience on application of the labelled antigens in enzyme immunoassay (EIA) is described.

Animals↗

PubMed1981

Isolation and properties of a lectin from the seeds of hairy vetch (Vicia villosa Roth).

The lectin of the seeds of hairy vetch (Vicia villosa Roth), which selectively binds murine cytotoxic T-lymphocytes, was purified by simple affinity-chromatographic procedures on two different N-acetyl-alpha-D-galactosaminyl-carriers. The lectin thus obtained is homogeneous on polyacrylamide-gel electrophoresis both in acid and alkaline media and has a mol. wt. of approx. 120000. The lectin molecule appears to comprise four subunits of equal electrophoretic mobility, contains 4.3% of covalently bound neutral sugar and 0.72 Mn and 0.94 Zn atoms respectively. The anti-(blood-group A1) specific erythroagglutinating activity of the lectin can be detected at a limit concentration of 15 microgram/ml and is inhibitable most effectively by N-acetyl-D-galactosamine.

Amino Acids↗

PubMedDate not supplied

Isolation and characterization of a hemagglutinin with affinity for lipopolysaccharides from plasma of the crayfish Pacifastacus leniusculus.

A hemagglutinin with a high specific activity against trypsinized rabbit erythrocytes was identified in plasma of the freshwater crayfish Pacifastacus leniusculus. The activity of this crayfish hemagglutinin could be inhibited by sialoglycoproteins such as porcine stomach mucin, bovine submaxillary mucin, fetuin, and ovalbumin. However, the involvement of sialic acid in its binding specificity could not be unambiguously proven. Furthermore, the hemagglutinating activity in the crayfish plasma could be specifically inhibited by lipopolysaccharide from E. coli K-235, which might indicate a recognition role for this hemagglutinin. This hemagglutinin, which accounts for less than 0.01% of the total plasma protein, was purified to near homogeneity using affinity chromatography on a Fetuin-Sepharose 4B column. The molecular mass of the unreduced protein as revealed by sodium dodecyl sulphate electrophoresis in polyacrylamide gel was found to be 420,000 Da. Upon reduction with dithiothreitol the hemagglutinin dissociated to several subunits with masses ranging from 65,000 to 80,000 Da. Affinoblotting with peroxidase labelled lectins indicated that the hemagglutinin was likely to be a glycoprotein.

Animals↗

PubMedDate not supplied

Functional and structural identification of a new lectin activity of Borrelia recurrentis spirochetes.

1. Haemagglutinating activity (HA) was found and characterized in lysate of the spirochete Borrelia recurrentis. 2. The highest HA was observed using native rabbit red blood cells (RBC), especially oxidized rabbit RBC. 3. In a haemagglutination inhibition test the HA showed an affinity with monosaccharides D-glucosamine, D-galactosamine and N-acetyl-D-mannosamine and several glycoproteins and polysaccharides. 4. An inhibitory effect was also achieved by mouse monoclonal antibody H 9724, polyclonal antibodies from B. recurrentis infected mice and with rabbit polyclonal antibodies directed against B. recurrentis HA. 5. B. recurrentis proteins components of 29, 33, 41 and 55 kDa were identified by immunoblotting as structural subunits of complex binding activity of a new agglutinin.

Animals↗