Search PubMed⌕ Search

Biomedical subjects

D Roelcke

Publications and source records attributed to D Roelcke.

At least 109 records · Page 6Linked to original sources
PubMed1977

Serological identification of the new cold agglutinin specificity anti-Gd.

The specificity anti-Gd of human cold autoagglutinins is characterized using untreated and enzyme-treated human red blood cells. Gd determinants of human RBC are resistant to proteases, but are inactivated by neuraminidase (RDE). In contrast, I/i determinants are not inactivated by proteases or RDE, while Pr1-3 determinants are inactivated by proteases and RDE, and Pra determinants are resistant to RDE, but are inactivated by proteases.

Agglutinins↗
PubMed1976

Anti-Pr3: serological and immunochemical identification of a new anti-Pr subspecificity.

A monoclonal IgM(kappa) anti-Pr cold agglutinin occurring after a rubella infection is shown to have the 'new' anti-Pr subspecificity anti-Pr3. Pr3 determinants are found on cat and sheep erythrocytes which lack Pr1 and Pr2 determinants. By carbodiimide treatment of human erythrocyte glycoproteins, which causes intramolecular coupling of N-acetylneuraminic acid carboxyl groups and nucleophilic centers of the glycoprotein backbone, Pr3 antigen activity is strongly increased, while Pr1 and Pr2 determinants are inactivated.

Adult↗
PubMed1975

[High titer cold agglutinins with anti-pr specificity after rubella infection (author's transl)].

High titer cold agglutinins (CA) after rubella infection are reported. When the rubella exanthema disappeared the clinical aspect of a cold agglutinin disease was observed. Three weeks after the appearance of the cutaneous eruption the CA titer reached a maximum of 1/8000, to then continuously fall off to normal values within 20 weeks. Double diffusion tests showed that the isolated CA were IgM proteins that possess only chi-type light chains. In spite of normal protein- and immunoelectrophoresis patterns obtained with whole serum samples, the isolated CA showed restricted electrophoretic mobility and a deformation of the precipitate typical for monoclonal immunoglobulins. In contrast to the common anti-I specificity of IgM CA, the IgM CA described showed anti-Pr specificity. Possible interrelations between CA specificities and types of germs inducing reactive cold agglutination are discussed.

Adult↗
PubMed1975

The I antigen of human red cell membrane.

A high-active I antigen was isolated from human red cells after papainization. Investigations on its chemical composition and its serological properties are reported. 1. The I antigen activity was clearly demonstrated by hemagglutination inhibition studies and by the immuno-double-diffusion with all available anti-I sera. 2. The I antigen did not react with other antibodies directed against red cell antigens thus proving its specificity. Any relationships to antigen activities within the Pr-1/Pr-2, MN, and ABO systems could be excluded. 3. The substance was shown to be a glycoprotein and not a glycolipid. This was confirmed by different delipidation procedures promoting always an increase of I activity. The delipidized material contained only traces of fatty acids, and did not move on thin-layer chromatography in solvent systems normally used for glycolipid development. 4. The I determinant resides on alkali-stable oligosaccharide chains. The main sugars are galactose and N-acetylglucosamine which might be involved in the immunodeterminants.

Amino Acids↗