Heterogeneity of Heavy (γ) Chain Preparations from Human γG-Immunoglobulins

Abstract

IN recent publications, Cohen¹ and Cohen and Porter² have presented evidence that light chain preparations from partially reduced and iodoacetamide-alkylated γ-globulins of several species are heterogeneous. In glycine-urea starch-gel electrophoresis, pH 7–8, some eight to ten electrophoretically distinct bands were separated. Under similar electrophoretic conditions the heavy (γ) chains migrated as a diffuse band showing approximately the same spread as the original γ-globulin. In contrast to the light chains, the heavy chains did not give a band pattern.