Nicolas Costea

Light-Chain Heterogeneity of Cold Agglutinins

Cold agglutinins with specificity to I or to i antigens of humanadult or cord-blood erythrocytes produced during the course of Mycoplasma pneumoniae infection and infectious mononucleosis contain light chains of K and L types. However, cold agglutinin isolated from the serums of patients with chronic cold-agglutinin hemolytic anemia contains only type K light chains. The experimental evidence suggests that some cold agglutinins contain both types of light chains in the same molecule.

Immune Hemolysis Due to Hydralazine

Excerpt A number of adverse effects have been reported in association with hydralazine therapy including hyperdynamic circulation with increased heart rate and cardiac output, an acute rheumatoid s...

Allelic Exclusion of Light Chain Allotypes in Rabbit IgM Cold Agglutinins

Summary The IgM cold agglutinins were produced by intravenous injection of heat killed L. monocytogenes 4b into rabbits heterozygous (b4b5 ) for the light polypeptide chains of immunoglobulins. The radiolabeled cold agglutinins were analyzed for the b4 and b5 allotypes. The percentage of b4 and b5 light chains precipitable was independent of the order of precipitation with anti-b4 and anti-5 indicating that the cold agglutinin IgM molecules carry either the b4 or b5 light chain but not both.

α-Galactoside Determinants of the I-Antigen.

Summary The I-antigen of rabbit and human A1I erythrocytes was found to be inactivated by a potent α-galactosidase, while its reactivity was not influenced by β-galactosidase. Experimentally produced rabbit cold agglutinins were inhibited by several α-galactosides or by incubation with heat killed L. monocytogenes, the antigen responsible for their production. However, α-galactosides did not inhibit the reactivity of two different human cold agglutinins with anti-I specificity. The differences between the reactivity of human and rabbit cold agglutinins could be ascribed to differences in the structure of the antibody combining site.