ISOELECTRIC SEPARATION OF URINARY BENCE-JONES PROTEINS AND LIGHT CHAINS OF HUMAN IGG

Urinary Bence-Jones proteins from three different patients and two preparations of light chains derived from normal, pooled human IgG either by oxidative sulfitolysis or reduction/alkylation were subjected to isoelectric separation in a vertical column containing a combined pH and density gradient. The Bence-Jones proteins could be shown to be heterogeneous in pH gradients covering 0.5 to 7 pH units. In narrow pH gradients the resolving power was improved. In pH gradients covering the range of pH 3–10 and in the presence of 5 M urea the light-chain preparations could be partially resolved into the bands well known from gel electrophoresis. © 1969, Taylor & Francis Group, LLC. All rights reserved.