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G VAN LEEUWEN

Publications and source records attributed to G VAN LEEUWEN.

14 recordsLinked to original sources
PubMed1959

Macroglobulinemia. III. The effect of mercaptoethanol on the antigenic structure of macroglobulins.

The monomers obtained by treating gamma(1)-macroglobulins with mercaptoethanol have proved to be antigenically different from normal 7S 7gamma-globulin. The depolymerization of the macroglobulins resulted in the loss of several antigenic determinants, although the monomers still cross-reacted with antisera against macroglobulins. Reaggregation of the monomers occasionally resulted in the reconstitution of some or all of the antigenic determinants that were lost during depolymerization. Repeated freezing and thawing of pathological macroglobulins in iodoacetate resulted in their complete antigenic destruction. Repeated freezing and thawing of one of the monomers in excess iodoacetate resulted in the degradation to a protein antigenically indistinguishable from Bence Jones protein. The other two monomers studied were stable under these conditions.

Antigens↗
PubMed1957

Macroglobulinemia. I. The antigenic relationship of pathological macroglobulins to normal gamma-globulins.

Highly purified pathological macroglobulins, which had been characterized electrophoretically and in the ultracentrifuge, were studied by the Ouchterlony gel diffusion technique. These macroglobulins were shown to be antigenically related to normal gamma(1)-macroglobulin (19S) as well as the 7S gamma-globulins. The pathological macroglobulins differ among each other and they are antigenically deficient when compared with the normal macroglobulin. There is no correlation between the macroglobulin's antigenic structure and its physico-chemical properties.

Antigens↗
PubMed1957

Macroglobulinemia. II. Antisera specific for pathological macroglobulins.

Rabbits were immunized with three highly purified macroglobulins, from patients with macroglobulinemia. The antisera reacted with two macroglobulins with sedimentation constants of 19S and 26S of homologous antigen, and cross-reacted with the 7S and 19S globulins of normal gamma(1)-globulin and the heterologous pathological 19S macroglobulins. Exhaustive absorption of these antisera with normal gamma-globulins rendered them specific for the homologous macroglobulins. The antigenic properties of the pathological macroglobulins indicate that these proteins are abnormal.

Animals↗